GO:0044861 protein transport into plasma membrane raft: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0044861 (protein transport into plasma membrane raft) describes the directed movement of a protein into a plasma membrane raft, a cholesterol- and sphingolipid-enriched ordered domain of the plasma membrane.
• Raft association is not a passive consequence of membrane mixing; it can determine whether a protein reaches the plasma membrane at all, as shown for the transmembrane protein linker for activation of T cells (LAT).
• ER exit sites and the COPII adaptor SEC24D selectively recruit raft-preferring proteins for rapid export from the endoplasmic reticulum, linking early secretory sorting to raft delivery.
• Palmitoylation and other lipid modifications act as sorting signals that direct proteins into rafts and support their plasma membrane transport.
• Raft-targeted transport is functionally important in cancer: recruitment of phosphorylated MET to lipid rafts via CD24 amplifies MET signaling and contributes to drug resistance in endometrial cancer cell lines.
• The process can be studied with imaging, proteomics, and CRISPR-based perturbation of candidate raft-trafficking genes, including SLC26A3, LAT, and SEC24D.
Description
GO:0044861, protein transport into plasma membrane raft, is a biological process term that captures the directed movement of a protein into a plasma membrane raft. Plasma membrane rafts are dynamic, cholesterol- and sphingolipid-enriched membrane domains that concentrate specific proteins and lipids, and they are now understood as platforms for signaling and membrane traffic rather than as static structures. The term therefore sits at the intersection of membrane trafficking and membrane organization: it asks how a protein is actively delivered to, or retained in, a raft domain at the cell surface. Understanding this process matters because raft localization can change a protein's signaling output, its interaction partners, and its stability at the plasma membrane. For example, raft association is a determinant of plasma membrane localization for certain proteins, and disrupting raft association can redirect a protein away from the surface. In T cells, palmitoylation-dependent plasma membrane transport of the linker for activation of T cells (LAT) is required for its surface delivery, even though raft-independent signaling functions have also been described. More recently, ER exit sites mediated by the COPII adaptor SEC24D were shown to selectively recruit lipid raft-preferring proteins for rapid ER export, providing a mechanistic link between early secretory sorting and raft-directed transport. In parallel, work on SLC26A3 showed that N-glycans do not significantly alter plasma membrane or lipid raft trafficking, but appear to stabilize interdomain contacts to stimulate transport, illustrating how cargo-specific features can modulate raft-related trafficking without being strictly required for raft targeting. Together, these studies make GO:0044861 a useful framework for researchers who need to distinguish raft-dependent from raft-independent transport routes and to test whether a candidate gene controls surface delivery of a raft-associated protein.
protein transport into plasma membrane raft At A Glance
| GO ID | GO:0044861 |
|---|---|
| GO term | protein transport into plasma membrane raft |
| Ontology | biological_process |
| Synonym | none listed |
| Definition | The directed movement of a protein into a plasma membrane raft. |
| Major function | Delivery and partitioning of proteins into cholesterol- and sphingolipid-enriched plasma membrane raft domains |
| Related cellular structure | Plasma membrane raft / lipid raft |
| Representative cargo | LAT, MET, SLC26A3, raft-preferring secretory proteins |
| Key sorting step | ER exit and secretory trafficking, including SEC24D-dependent ER exit site recruitment |
| Common regulatory modification | Palmitoylation and other lipid modifications that promote raft association |
What Is GO:0044861?
In plain terms, GO:0044861 describes the process by which a protein is moved into a plasma membrane raft. A plasma membrane raft is a small, ordered, cholesterol- and sphingolipid-rich patch within the plasma membrane, and proteins that partition into these patches often use specific sorting signals, such as lipid modifications or transmembrane domain features, to get there. The term is narrower than general plasma membrane protein transport because it specifies the destination as a raft domain, and it is narrower than raft assembly because it focuses on the protein cargo being delivered into the raft. The directed movement can occur during biosynthetic delivery from the secretory pathway, during endocytic recycling back to the surface, or through lateral partitioning within the plasma membrane, and the QuickGO definition intentionally covers the directed movement of a protein into a plasma membrane raft without committing to a single route.
Why Is protein transport into plasma membrane raft Important in Cell Biology?
GO:0044861 is important because raft localization is not a trivial detail of membrane biology; it can determine whether a protein reaches the plasma membrane, how long it stays there, and what signaling complexes it assembles. Raft association has been shown to be a determinant of plasma membrane localization, meaning that defects in raft-directed transport can mislocalize proteins and alter cell behavior. In immune cells, palmitoylation-dependent plasma membrane transport of LAT is required for its surface expression, connecting raft trafficking to T cell signaling. In cancer, recruitment of phosphorylated MET to lipid rafts via CD24 amplifies the MET signaling cascade and leads to drug resistance in endometrial cancer cell lines, directly linking raft transport to therapeutic resistance. At the cell biological level, ER exit sites mediated by the COPII adaptor SEC24D selectively recruit lipid raft-preferring proteins for rapid ER export, showing that raft-directed transport begins early in the secretory pathway and is actively sorted. Finally, because raft trafficking can be modulated by cargo-specific features such as N-glycans on SLC26A3, the process is a rich source of hypotheses for genetic and pharmacological intervention.
• Raft association can determine plasma membrane localization, so GO:0044861 is central to understanding protein targeting.
• Palmitoylation-dependent plasma membrane transport of LAT links raft trafficking to T cell signaling.
• Recruitment of phosphorylated MET to lipid rafts via CD24 amplifies MET signaling and causes drug resistance in endometrial cancer cell lines.
• SEC24D-mediated ER exit sites selectively recruit raft-preferring proteins for rapid ER export, connecting early secretion to raft delivery.
• Lipid rafts and membrane traffic are broadly linked, making GO:0044861 relevant to endocytosis, recycling, and polarized transport.
• N-glycans on SLC26A3 do not significantly alter plasma membrane or lipid raft trafficking but stabilize interdomain contacts, showing cargo-specific modulation.
• Raft-preferring proteins can be sorted at ER exit sites, which has implications for secretory pathway engineering.
• Raft domains are cholesterol- and sphingolipid-enriched, so lipid metabolism and membrane composition influence this process.
• Raft trafficking is a potential target for overcoming drug resistance in cancers with RTK signaling.
• The process can be interrogated with CRISPR KO, point mutation, knock-in, and overexpression models of candidate genes.
What Happens During protein transport into plasma membrane raft?
Cargo recognition and sorting at ER exit sites
In simple terms: Before a protein can reach a raft at the cell surface, it must first be selected for export from the endoplasmic reticulum.
The first stage of protein transport into plasma membrane raft is the recognition of raft-preferring cargo at ER exit sites. ER exit sites mediated by the COPII adaptor SEC24D selectively recruit lipid raft-preferring proteins for rapid ER export, which means that raft-destined proteins can be sorted early in the secretory pathway rather than after reaching the Golgi. This selective recruitment provides a mechanism by which raft-preferring proteins are concentrated into transport carriers, and it links the COPII machinery to the eventual delivery of proteins into plasma membrane rafts. Cargo-specific features, such as N-glycans on SLC26A3, can modulate this trafficking step, although in that case N-glycans did not significantly alter plasma membrane or lipid raft trafficking and instead appeared to stabilize interdomain contacts to stimulate transport.
Vesicular transport through the secretory pathway
In simple terms: After sorting, the protein travels in membrane carriers through the secretory pathway toward the cell surface.
Once raft-preferring cargo is selected at ER exit sites, it moves through the secretory pathway in vesicular carriers. Lipid rafts and membrane traffic are intimately connected, and raft-associated proteins can use the same secretory and endocytic routes as other membrane proteins while being enriched in specific carriers. The directed movement of a protein into a plasma membrane raft therefore depends on the general machinery of membrane traffic, but with sorting information that biases the cargo toward raft domains. This stage is where palmitoylation and other lipid modifications can act as sorting signals; for LAT, palmitoylation-dependent plasma membrane transport is required for surface delivery, even though raft-independent signaling functions have also been described.
Arrival at the plasma membrane and raft partitioning
In simple terms: When the protein reaches the plasma membrane, it must partition into the raft domain rather than staying in the surrounding membrane.
At the plasma membrane, the delivered protein must partition into the raft domain to complete GO:0044861. Raft association is a determinant of plasma membrane localization, and proteins that fail to associate with rafts can be mislocalized or retained intracellularly. The plasma membrane raft is a cholesterol- and sphingolipid-enriched ordered domain, and the physical properties of the protein, including its transmembrane domain and lipid modifications, influence whether it enters the raft. Lipid self-assembly and lectin-induced reorganization of the plasma membrane can further reshape raft organization, which in turn affects how proteins are accommodated within rafts.
Raft-dependent signaling and functional consequences
In simple terms: Once in the raft, the protein can assemble signaling complexes that change cell behavior.
The functional endpoint of protein transport into plasma membrane raft is often the assembly of signaling complexes within the raft. In endometrial cancer cell lines, recruitment of phosphorylated MET to lipid rafts via CD24 amplifies the MET signaling cascade and leads to drug resistance, showing that raft delivery can directly alter therapeutic response. In T cells, LAT is a raft-associated adaptor whose palmitoylation-dependent plasma membrane transport is required for its surface expression, linking raft trafficking to T cell activation. These examples illustrate that GO:0044861 is not merely a trafficking curiosity but a process that shapes signal transduction and disease phenotypes.
Cargo-specific modulation and quality control
In simple terms: Different proteins can have different requirements for raft transport, and some features stabilize the cargo rather than being strictly required for raft targeting.
Not every cargo feature is essential for raft transport. For SLC26A3, N-glycans do not significantly alter plasma membrane or lipid raft trafficking, but they appear to stabilize interdomain contacts to stimulate transport, indicating that some modifications support function or stability rather than raft targeting itself. This cargo-specific modulation means that researchers studying GO:0044861 should test each candidate protein individually rather than assuming a universal raft-trafficking code. The broader principle is that raft association and plasma membrane localization are related but separable properties, and both need to be measured.
Key Genes Involved in GO:0044861 protein transport into plasma membrane raft
The following genes and proteins have been experimentally linked to raft-associated transport, raft localization, or raft-dependent signaling in the verified literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| LAT | Palmitoylation-dependent plasma membrane transport; raft-associated adaptor in T cells | Model for testing whether raft association is required for surface delivery |
| MET | Receptor tyrosine kinase recruited to lipid rafts via CD24; amplified signaling | Model for raft-dependent drug resistance in endometrial cancer cell lines |
| CD24 | Recruits phosphorylated MET to lipid rafts | Model for raft-mediated RTK signaling and resistance |
| SLC26A3 | Chloride/bicarbonate exchanger whose N-glycans modulate trafficking and transport | Model for cargo-specific modulation of plasma membrane and lipid raft trafficking |
| SEC24D | COPII adaptor mediating ER exit sites that recruit raft-preferring proteins | Model for early secretory sorting of raft-destined cargo |
| SEC24A | COPII component family member relevant to ER export | Comparative model for COPII-dependent raft cargo selection |
| SEC24B | COPII component family member relevant to ER export | Comparative model for COPII-dependent raft cargo selection |
| SEC24C | COPII component family member relevant to ER export | Comparative model for COPII-dependent raft cargo selection |
| COPII coat components | Generate ER-derived carriers for secretory cargo | Model for linking ER export to raft delivery |
| Raft-preferring secretory proteins | Cargo class enriched in ER exit sites | Model for testing selective recruitment |
| Plasma membrane ATPase (yeast Pma1) | Lipid-dependent surface transport model in yeast | Model for plasma membrane biogenesis and raft-related transport |
| Sphingolipid biosynthetic enzymes | Determine raft lipid composition | Model for testing how lipid environment affects raft transport |
| Cholesterol biosynthesis enzymes | Determine raft cholesterol content | Model for testing raft integrity and protein partitioning |
| Palmitoyl transferases | Add palmitate to cargo proteins such as LAT | Model for lipid modification-dependent raft transport |
| Lectin-type raft probes | Reorganize plasma membrane rafts | Model for studying raft dynamics and protein entry |
| Membrane traffic regulators | Control vesicular transport to the plasma membrane | Model for dissecting secretory versus endocytic routes to rafts |
How Is protein transport into plasma membrane raft Regulated?
Regulation of protein transport into plasma membrane raft occurs at multiple levels. Cargo selection at ER exit sites is regulated by the COPII adaptor SEC24D, which selectively recruits lipid raft-preferring proteins for rapid ER export. Lipid modification, particularly palmitoylation, regulates plasma membrane transport of cargo such as LAT. The lipid composition of the membrane, including cholesterol and sphingolipids, determines raft formation and therefore the availability of raft domains for incoming proteins. Lectin-induced reorganization of the plasma membrane can also reshape raft organization and influence protein partitioning. Finally, cargo-specific features such as N-glycans on SLC26A3 can modulate trafficking and transport without being strictly required for raft targeting, indicating that regulation is protein-specific.
protein transport into plasma membrane raft and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| MET | Drug resistance in endometrial cancer via raft-recruited phosphorylated MET | Endometrial cancer cell lines with MET overexpression or point mutation; raft fractionation and drug response assays |
| CD24 | Raft-mediated MET signaling and resistance | CD24 knockout and overexpression in cancer cell lines; co-immunoprecipitation and raft isolation |
| LAT | T cell signaling and surface expression | LAT palmitoylation-site point mutants and knockout T cell lines; surface biotinylation and raft fractionation |
| SLC26A3 | Epithelial transport and trafficking modulation by N-glycans | SLC26A3 glycosylation-site mutants and knockout epithelial cells; transport assays and raft fractionation |
| SEC24D | ER exit site-mediated raft cargo sorting | SEC24D knockout and tagged knock-in cells; live imaging of ER exit sites and raft cargo export |
Cancer drug resistance and raft-dependent RTK signaling
Raft transport can directly contribute to cancer drug resistance. In endometrial cancer cell lines, the MET signaling cascade is amplified by recruitment of phosphorylated MET to lipid rafts via CD24, and this leads to drug resistance. This finding places GO:0044861 at the center of efforts to understand how raft localization of receptor tyrosine kinases changes therapeutic response, and it suggests that disrupting raft delivery or raft association of MET could resensitize resistant cells. Because raft association is a determinant of plasma membrane localization, mislocalization of raft-associated oncoproteins may also alter signaling output in other cancers.
Immune signaling and T cell function
Raft trafficking is important for immune cell signaling. LAT requires palmitoylation-dependent plasma membrane transport for its surface expression, and LAT is a raft-associated adaptor in T cells. Although raft-independent signaling functions of LAT have been described, the transport step itself is a regulated process that determines how much LAT reaches the surface. This makes GO:0044861 relevant to understanding T cell activation and to interpreting phenotypes caused by mutations that affect LAT trafficking.
Epithelial transport and channel/exchanger trafficking
Raft-related trafficking also affects epithelial transport proteins. SLC26A3 is a chloride/bicarbonate exchanger whose N-glycans do not significantly alter plasma membrane or lipid raft trafficking but appear to stabilize interdomain contacts to stimulate transport. This example shows that disease-relevant transport defects can arise from changes in protein stability or domain contacts rather than from altered raft targeting, and it highlights the need to separate raft trafficking from other trafficking steps when interpreting disease variants.
Membrane trafficking disorders and secretory pathway dysfunction
Because raft-directed transport begins at ER exit sites and proceeds through the secretory pathway, defects in COPII-dependent sorting can affect raft cargo delivery. Lipid rafts and membrane traffic are broadly connected, so perturbations in membrane traffic machinery can alter raft protein localization and signaling. In yeast, lipid-dependent surface transport of the proton pumping ATPase has been used as a model to study plasma membrane biogenesis, providing a genetically tractable system for dissecting raft-related transport defects.
From protein transport into plasma membrane raft-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is a candidate gene required for delivery of a raft-associated protein to the plasma membrane? | CRISPR knockout of the candidate gene followed by surface biotinylation and raft fractionation |
| Does a specific palmitoylation site control raft transport? | Point mutation of the palmitoylation site (e.g., in LAT) and comparison of surface delivery |
| Does a disease-associated variant alter raft trafficking? | Knock-in of the variant into the endogenous locus and measurement of raft localization |
| Where does a raft cargo encounter sorting machinery? | Tagged knock-in of the cargo and live imaging of ER exit sites and secretory carriers |
| Does overexpression of a raft cargo saturate or alter raft transport? | Inducible overexpression of the cargo and quantification of raft partitioning |
| Does lipid composition control raft transport? | CRISPR knockout of sphingolipid or cholesterol biosynthetic enzymes and raft analysis |
How to Study the protein transport into plasma membrane raft Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Detergent-resistant membrane fractionation | Partitioning of proteins into raft domains | Testing whether a cargo protein enters rafts |
| Surface biotinylation | Amount of protein at the plasma membrane | Distinguishing transport defects from raft association defects |
| Live-cell imaging of ER exit sites | Recruitment and export kinetics of raft-preferring cargo | Testing SEC24D-dependent sorting |
| Single-molecule tracking / FRAP | Lateral mobility and raft partitioning at the plasma membrane | Measuring raft dynamics and protein entry |
| Mass spectrometry proteomics | Protein composition of raft versus non-raft fractions | Discovering raft cargo and sorting dependencies |
| Phospho-signaling assays | Activation of raft-dependent signaling pathways | Linking raft transport to MET or LAT signaling |
| Drug sensitivity assays | Cell viability under targeted therapy | Testing whether raft transport drives resistance |
| Glycosylation-site mutagenesis | Contribution of N-glycans to trafficking and stability | Dissecting cargo-specific modulation of raft transport |
Membrane fractionation and raft isolation
Biochemical raft isolation, typically by detergent-resistant membrane preparation or density gradient centrifugation, is the classic method to determine whether a protein partitions into rafts. This approach can be combined with surface biotinylation to distinguish proteins that have reached the plasma membrane from those retained intracellularly, which is essential for studying GO:0044861. For cargo such as LAT, raft fractionation alongside surface labeling can reveal whether a palmitoylation mutant fails at the transport step or at the raft association step.
Imaging of secretory carriers and ER exit sites
Live-cell imaging of ER exit sites and secretory carriers allows researchers to visualize the route taken by raft-preferring proteins. SEC24D-mediated ER exit sites selectively recruit lipid raft-preferring proteins for rapid ER export, and imaging can quantify the kinetics of this recruitment. Fluorescence recovery after photobleaching and single-molecule tracking can further measure lateral mobility and raft partitioning at the plasma membrane. These methods are particularly useful for testing whether a candidate gene affects the rate or fidelity of raft-directed transport.
Proteomics of raft and non-raft fractions
Mass spectrometry-based proteomics of raft versus non-raft membrane fractions can identify the protein composition of raft domains and quantify changes after genetic perturbation. This is useful for discovering new cargo proteins that depend on specific sorting factors, such as SEC24D, for raft delivery. Proteomic comparison of wild-type and knockout cells can also reveal compensatory changes in membrane trafficking that might mask a transport defect.
Functional signaling assays
Because raft transport often serves signaling, functional assays are needed to connect trafficking to phenotype. In endometrial cancer cell lines, raft recruitment of phosphorylated MET via CD24 amplifies MET signaling and leads to drug resistance, so phospho-MET quantification and drug sensitivity assays are appropriate readouts. In T cells, LAT-dependent signaling assays can test whether altered raft transport changes activation. These functional assays complement imaging and biochemical fractionation and help establish causality.
How CRISPR Can Be Used to Study GO:0044861 protein transport into plasma membrane raft
Knockout
CRISPR knockout is used to remove a candidate gene and test whether it is required for protein transport into plasma membrane rafts. For example, knocking out SEC24D can test whether ER exit site-mediated recruitment of raft-preferring proteins is necessary for their rapid ER export. Knocking out LAT or its palmitoyl transferase can reveal whether surface delivery of this raft-associated adaptor depends on the modified protein. Knockout of lipid biosynthetic enzymes can test whether raft lipid composition is required for cargo partitioning.
Point Mutation
Point mutation is used to dissect specific residues or modification sites that control raft transport. Mutating the palmitoylation site of LAT is a classic approach to test whether lipid modification is required for plasma membrane transport. Point mutations in SLC26A3 glycosylation sites can test whether N-glycans modulate trafficking or stability without affecting raft targeting. Disease-associated point mutations in raft cargo or sorting machinery can be introduced to test their effect on raft delivery.
Knock-in
Knock-in of tags or disease variants allows raft transport to be studied at endogenous expression levels. Tagged knock-in of a raft cargo enables live imaging of its route from ER exit sites to the plasma membrane. Knock-in of a disease-associated variant, such as a MET or CD24 variant, can test whether the variant alters raft recruitment and signaling. Knock-in of a glycosylation-site variant in SLC26A3 can test its effect on transport and stability in a physiological context.
Overexpression
Overexpression is used to ask whether increasing the amount of a raft cargo or sorting factor changes raft transport. Overexpression of MET or CD24 can amplify raft-dependent signaling and drug resistance phenotypes in cancer cell lines. Overexpression of raft-preferring secretory proteins can test whether the ER exit site machinery becomes saturated. Overexpression of LAT can test whether surface delivery is limited by transport capacity or by raft availability.
How EDITGENE Supports protein transport into plasma membrane raft Research
Researchers studying protein transport into plasma membrane raft-related genes often need to determine whether a candidate gene is causally involved in raft delivery, raft partitioning, or raft-dependent signaling. Establishing causality requires controlled genetic perturbation, ideally at the endogenous locus, combined with quantitative readouts of surface transport and raft association. EDITGENE provides the CRISPR cell model and screening services needed to move from correlation to mechanism in this pathway.
Contact EDITGENE today to design your custom CRISPR model for protein transport into plasma membrane raft research.
Frequently Asked Questions About protein transport into plasma membrane raft
What is GO:0044861 protein transport into plasma membrane raft?
GO:0044861 is a biological process term defined as the directed movement of a protein into a plasma membrane raft, a cholesterol- and sphingolipid-enriched ordered membrane domain.
What is a plasma membrane raft?
A plasma membrane raft is a small, ordered, cholesterol- and sphingolipid-rich domain within the plasma membrane that concentrates specific proteins and lipids and serves as a platform for signaling and trafficking.
What genes are involved in protein transport into plasma membrane raft?
Genes studied in this context include LAT, MET, CD24, SLC26A3, and SEC24D, based on published experimental evidence.
How is raft association related to plasma membrane localization?
Raft association is a determinant of plasma membrane localization, meaning that proteins which fail to associate with rafts can be mislocalized or retained inside the cell.
Does palmitoylation control raft transport?
Yes, palmitoylation-dependent plasma membrane transport has been demonstrated for LAT, although raft-independent signaling functions have also been described.
What is the role of SEC24D in raft transport?
SEC24D mediates ER exit sites that selectively recruit lipid raft-preferring proteins for rapid ER export, linking early secretory sorting to raft delivery.
How does raft transport contribute to cancer drug resistance?
Recruitment of phosphorylated MET to lipid rafts via CD24 amplifies MET signaling and leads to drug resistance in endometrial cancer cell lines.
Do N-glycans affect lipid raft trafficking?
For SLC26A3, N-glycans do not significantly alter plasma membrane or lipid raft trafficking, but they appear to stabilize interdomain contacts to stimulate transport.
How can I study protein transport into plasma membrane rafts?
Common approaches include detergent-resistant membrane fractionation, surface biotinylation, live-cell imaging of ER exit sites, proteomics, and functional signaling assays.
What CRISPR models are useful for studying GO:0044861?
Knockout, point mutation, knock-in, and overexpression models of cargo proteins and sorting factors such as LAT, SEC24D, MET, and CD24 are useful for dissecting raft transport mechanisms.
Conclusion
GO:0044861, protein transport into plasma membrane raft, describes a directed trafficking process that delivers proteins into cholesterol- and sphingolipid-enriched raft domains. The process begins with cargo sorting at ER exit sites, proceeds through the secretory pathway, and ends with raft partitioning and raft-dependent signaling at the plasma membrane. Experimental evidence links this process to immune cell signaling through LAT, to cancer drug resistance through raft-recruited MET, and to cargo-specific modulation through SLC26A3 glycosylation. Because raft association can determine plasma membrane localization, defects in this pathway have broad implications for cell biology and disease. Researchers can now dissect GO:0044861 using CRISPR knockout, point mutation, knock-in, and overexpression models combined with raft fractionation, imaging, proteomics, and functional assays.
References
- 1. Achilles S et al.. 2025. N-glycans on SLC26A3 do not significantly alter plasma membrane or lipid raft trafficking, but appear to stabilize interdomain contacts to stimulate transport.. Am J Physiol Gastrointest Liver Physiol 329(5):G628-G638 PMID: 41071686
- 2. Diaz-Rohrer BB et al.. 2014. Membrane raft association is a determinant of plasma membrane localization.. Proc Natl Acad Sci U S A 111(23):8500-5 PMID: 24912166
- 3. Ono YJ et al.. 2015. Met Signaling Cascade Is Amplified by the Recruitment of Phosphorylated Met to Lipid Rafts via CD24 and Leads to Drug Resistance in Endometrial Cancer Cell Lines.. Mol Cancer Ther 14(10):2353-63 PMID: 26227486
- 4. Hundt M et al.. 2009. Palmitoylation-dependent plasma membrane transport but lipid raft-independent signaling by linker for activation of T cells.. J Immunol 183(3):1685-94 PMID: 19592663
- 5. Sych T et al.. 2018. Lipid self-assembly and lectin-induced reorganization of the plasma membrane.. Philos Trans R Soc Lond B Biol Sci 373(1747) PMID: 29632269
- 6. Castello-Serrano I et al.. 2025. ER exit sites mediated by the COPII adaptor sec24D selectively recruit lipid raft-preferring proteins for rapid ER export.. Nat Commun 16(1):10694 PMID: 41309618
- 7. Hanzal-Bayer MF et al.. 2007. Lipid rafts and membrane traffic.. FEBS Lett 581(11):2098-104 PMID: 17382322
- 8. Toulmay A et al.. 2007. Lipid-dependent surface transport of the proton pumping ATPase: a model to study plasma membrane biogenesis in yeast.. Biochimie 89(2):249-54 PMID: 16938383
