GO:1905793 protein localization to pericentriolar material: Components, Assembly and Research Methods, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:1905793 describes the directed transport or retention of proteins within the pericentriolar material (PCM), the electron-dense matrix that surrounds centrioles and nucleates microtubules.
• PCM protein localization is cell-cycle dependent and is regulated by phosphorylation and acetylation switches that control centrosome maturation.
• The PCM scaffold not only anchors proteins but also enables RNA localization to centrosomes, linking protein localization to local translation.
• Centriolar satellite proteins such as Cep72 are recruited to the PCM by the MLL/WDR5 complex to regulate microtubule nucleation and spindle formation.
• Defects in PCM protein localization are associated with cancer, ciliopathies, and developmental disorders, making this process a target for CRISPR-based disease modeling [1,5,6].
• CRISPR knockout, point-mutation, knock-in, and overexpression models are essential to dissect the causal roles of PCM-localized proteins in cell division and disease [3,7].
Description
The pericentriolar material (PCM) is a dynamic, electron-dense matrix that surrounds the centrioles and serves as the primary microtubule-organizing center in animal cells. The process by which proteins are transported to, or maintained within, this matrix is annotated as GO:1905793, protein localization to pericentriolar material. This biological process is fundamental for centrosome maturation, mitotic spindle assembly, and proper cell division [4,8]. Researchers studying cell cycle control, cytoskeletal dynamics, and ciliogenesis require a precise understanding of how PCM proteins are targeted and retained, because mislocalization of even a single component can disrupt spindle polarity and chromosome segregation [3,7]. Recent work has shown that the PCM scaffold is not a passive anchor but an active platform that enables RNA localization and local protein synthesis, expanding the functional repertoire of this compartment. Moreover, the recruitment of centriolar satellite proteins such as Cep72 to the PCM by the MLL/WDR5 complex highlights the interplay between chromatin-modifying machinery and centrosome function. Given the growing links between PCM protein localization and human diseases including cancer and ciliopathies, this article synthesizes current evidence on the mechanisms, key genes, and research methods used to study GO:1905793 [1,5,6].
protein localization to pericentriolar material At A Glance
| GO ID | GO:1905793 |
|---|---|
| GO term | protein localization to pericentriolar material |
| Ontology | biological_process |
| Synonym | protein localisation in pericentriolar material; protein localisation to pericentriolar material; protein localization in pericentriolar material |
| Major function | Transport and retention of proteins within the pericentriolar material to support centrosome maturation, microtubule nucleation, and spindle assembly |
| Related cellular component | Pericentriolar material (PCM) |
| Related biological processes | Centrosome maturation, mitotic spindle organization, ciliogenesis |
| Key regulatory mechanism | Cell cycle-dependent phosphorylation and acetylation of PCM proteins |
| Disease relevance | Cancer, ciliopathies, developmental disorders |
What Is GO:1905793?
GO:1905793, protein localization to pericentriolar material, is defined as a process in which a protein is transported to, or maintained in, a location within a pericentriolar material. This includes both the active delivery of proteins to the PCM and the mechanisms that retain them there, ensuring the correct spatiotemporal composition of the centrosomal matrix. The term is a biological process and is synonymous with protein localisation in pericentriolar material, protein localisation to pericentriolar material, and protein localization in pericentriolar material.
Why Is protein localization to pericentriolar material Important in Cell Biology?
Protein localization to the pericentriolar material is essential for the structural and functional integrity of the centrosome, which acts as the primary microtubule-organizing center in animal cells. Without the correct complement of PCM proteins, cells fail to assemble a bipolar spindle, leading to chromosome missegregation, aneuploidy, and cell death. This process is also critical for ciliogenesis, as PCM proteins such as CEP290 and CCHCR1 are required for the formation of primary cilia, and their mislocalization is linked to ciliopathies [5,6]. Furthermore, the PCM scaffold enables RNA localization to centrosomes, suggesting a role in local translation and cell fate determination. Understanding GO:1905793 therefore has broad implications for developmental biology, cancer research, and regenerative medicine.
• Ensures proper centrosome maturation and mitotic spindle assembly.
• Regulates microtubule nucleation and spindle formation through centriolar satellite proteins like Cep72.
• Supports ciliogenesis by localizing proteins such as CEP290 and CCHCR1 to the PCM [5,6].
• Enables RNA localization to centrosomes, linking protein localization to local translation.
• Its dysregulation is associated with cancer, including centrosome amplification and aneuploidy [1,3].
• Cell cycle progression is controlled by CDK activity at the centrosome, which regulates PCM protein localization.
• Mutations in PCM proteins cause developmental disorders and ciliopathies [5,6].
• Provides a target for CRISPR-based disease modeling and therapeutic intervention.
• Helps explain cell-type-specific differences in PCM regulation.
• Offers insights into the evolution of centrosome function through gene duplication studies.
What Happens During protein localization to pericentriolar material?
Recruitment of centriolar satellite proteins to the PCM
In simple terms: Proteins that normally float near the centrioles are actively moved into the surrounding matrix.
Centriolar satellites are small granules that cluster around the centrosome. The MLL/WDR5 complex recruits the centriolar satellite protein Cep72 to the PCM, where it regulates microtubule nucleation and spindle formation. This recruitment is essential for proper mitotic progression, as loss of Cep72 or its upstream regulators leads to spindle defects. The process is dynamic and cell-cycle dependent, with satellites delivering proteins to the PCM during centrosome maturation.
Cell cycle-dependent maturation of the PCM
In simple terms: The matrix around the centrioles grows and changes composition as the cell prepares to divide.
During G2/M transition, the PCM expands and recruits additional proteins such as pericentrin and CDK5RAP2. A cell cycle-dependent transition from acetylation to phosphorylation regulates timely centrosome maturation, ensuring that PCM proteins are localized at the right time. CDK activity at the centrosome further controls this process, and inhibition of CDKs prevents PCM expansion. This maturation step is critical for bipolar spindle assembly and accurate chromosome segregation [3,8].
Scaffold-mediated retention and RNA localization
In simple terms: The PCM acts like a sticky scaffold that holds proteins and even RNA in place.
The PCM scaffold, composed of proteins such as pericentrin and CEP192, not only anchors proteins but also enables RNA localization to centrosomes. This scaffold provides binding sites for RNA-binding proteins and their cargo, linking protein localization to local translation. Disruption of the scaffold leads to loss of PCM integrity and mislocalization of both proteins and RNA. This dual role highlights the PCM as a multifunctional hub for centrosome function.
Regulation by phosphorylation and acetylation
In simple terms: Chemical tags on proteins act as switches to control when they move into the matrix.
Post-translational modifications regulate the localization of PCM proteins. A cell cycle-dependent transition from acetylation to phosphorylation controls timely centrosome maturation, with specific residues on PCM proteins being modified to promote or inhibit their recruitment. CDK activity at the centrosome also phosphorylates PCM components, and this phosphorylation is required for their localization. These modifications ensure that PCM assembly is tightly coupled to the cell cycle [3,8].
CPAP and centriole duplication fidelity
In simple terms: A protein called CPAP helps build new centrioles, and when it is missing, the matrix becomes abnormal.
CPAP insufficiency leads to incomplete centrioles that duplicate but fragment, resulting in disrupted PCM organization. This fragmentation impairs the localization of PCM proteins and leads to mitotic defects. CPAP thus plays a critical role in maintaining centriole integrity, which in turn is required for proper PCM protein localization.
Key Genes Involved in GO:1905793 protein localization to pericentriolar material
The following genes encode proteins that are localized to the pericentriolar material or regulate that localization, and they are frequently studied in the context of GO:1905793.
| Gene | Major Role | Research Relevance |
|---|---|---|
| Cep72 | Centriolar satellite protein recruited to PCM by MLL/WDR5; regulates microtubule nucleation | Spindle formation, cancer |
| CPAP | Centriole duplication and integrity; required for PCM organization | Centriole fragmentation, mitotic defects |
| CDK5RAP2 | PCM scaffold protein; regulates centrosome maturation | Cell cycle, microcephaly |
| CEP290 | PCM protein with non-ciliary functions; interacts with focal adhesion proteins | Ciliopathies, retinal degeneration |
| CCHCR1 | Links P-body proteins to centrosome; required for ciliogenesis via OFD1 and PCM1 | Ciliogenesis, cancer |
| PCM1 | Major PCM scaffold protein; anchors centriolar satellites | Centrosome assembly, ciliogenesis |
| OFD1 | Centriolar protein; interacts with CCHCR1 and PCM1 | Oral-facial-digital syndrome |
| WDR5 | Component of MLL complex; recruits Cep72 to PCM | Chromatin regulation, spindle assembly |
| MLL | Histone methyltransferase; part of complex recruiting Cep72 | Leukemia, spindle formation |
| Pericentrin | PCM scaffold protein; recruits CDK5RAP2 and others | Centrosome maturation, cancer |
| CEP192 | PCM scaffold protein; essential for PCM assembly | Mitosis, centrosome amplification |
| Spd-2 | PCM protein; gene duplication reveals cell-type-specific regulation | Evolution, cell-type-specific PCM |
| CDK1 | Cyclin-dependent kinase; phosphorylates PCM proteins | Cell cycle regulation |
| CDK2 | Cyclin-dependent kinase; regulates centrosome duplication | Cell cycle, cancer |
| Aurora A | Kinase that promotes PCM maturation | Mitosis, cancer |
| Plk1 | Kinase that regulates centrosome maturation | Mitosis, cancer |
| SAS-6 | Centriole assembly protein; influences PCM recruitment | Centriole duplication |
How Is protein localization to pericentriolar material Regulated?
The localization of proteins to the pericentriolar material is tightly regulated by cell cycle-dependent post-translational modifications. A key regulatory switch involves the transition from acetylation to phosphorylation of PCM proteins, which controls timely centrosome maturation. CDK activity at the centrosome, particularly CDK1 and CDK2, phosphorylates multiple PCM components to promote their recruitment during G2/M. Aurora A and Plk1 kinases also regulate PCM assembly and are themselves localized to the PCM. Additionally, the MLL/WDR5 complex recruits centriolar satellite proteins such as Cep72 to the PCM, linking chromatin-modifying machinery to centrosome function. This multi-layered regulation ensures that PCM protein localization is coordinated with cell cycle progression and that defects are sensed by checkpoint mechanisms [3,8].
protein localization to pericentriolar material and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| CPAP | Centriole fragmentation, mitotic defects, cancer | Knockout in HeLa or RPE1 cells |
| CEP290 | Joubert syndrome, Leber congenital amaurosis, ciliopathies | Point mutation knock-in in iPSCs |
| CCHCR1 | Ciliogenesis defects, cancer | Knockout in hTERT-RPE1 cells |
| Cep72 | Spindle defects, cancer | Overexpression and knockout in cancer cell lines |
| Spd-2 | Cell-type-specific PCM regulation | Gene duplication models in Drosophila |
Cancer and genomic instability
Dysregulation of PCM protein localization leads to centrosome amplification, multipolar spindles, and chromosome missegregation, all of which are hallmarks of cancer [1,3]. CPAP insufficiency causes centriole fragmentation and mitotic defects that can drive aneuploidy. CDK activity at the centrosome is often deregulated in cancer, contributing to uncontrolled proliferation. Targeting PCM protein localization pathways may offer therapeutic opportunities for cancers with centrosome amplification [1,3].
Ciliopathies and developmental disorders
Proper PCM protein localization is required for ciliogenesis. CEP290 mutations cause ciliopathies such as Joubert syndrome and Leber congenital amaurosis, and its non-ciliary functions at focal adhesions are also affected. CCHCR1 interacts with OFD1 and PCM1 to regulate ciliogenesis, and its dysfunction is linked to ciliopathy-like phenotypes. These findings highlight the importance of PCM protein localization in developmental signaling and tissue homeostasis [5,6].
Cell-type-specific PCM regulation and evolution
Gene duplication of Spd-2 has revealed cell-type-specific regulation of PCM, suggesting that different tissues may have distinct requirements for PCM protein localization. This has implications for understanding tissue-specific diseases and for developing targeted therapies that account for cell-type differences.
From protein localization to pericentriolar material-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of Cep72 disrupt PCM protein localization? | CRISPR knockout in HeLa cells |
| Does a specific phosphorylation site on pericentrin regulate PCM recruitment? | Point mutation knock-in in RPE1 cells |
| Can wild-type CPAP rescue centriole fragmentation? | Knock-in of tagged CPAP in CPAP-null cells |
| Where does CCHCR1 localize in live cells? | Tagged knock-in with GFP in hTERT-RPE1 cells |
| Does overexpression of CDK5RAP2 cause centrosome amplification? | Overexpression in U2OS cells |
| Does CEP290 mutation affect focal adhesion dynamics? | Point mutation knock-in in fibroblasts |
How to Study the protein localization to pericentriolar material Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Immunofluorescence | Localization of endogenous PCM proteins | Centrosome maturation studies |
| Live-cell imaging | Dynamic recruitment of tagged PCM proteins | Cell cycle-dependent localization |
| Proximity labeling (BioID) | Protein-protein interactions at the PCM | Identifying novel PCM components |
| CRISPR knockout screen | Genes required for PCM protein localization | Discovery of regulators |
| RNA FISH | Localization of RNAs to centrosomes | PCM scaffold function |
| Mass spectrometry | Proteomic composition of isolated centrosomes | PCM protein identification |
| Phospho-proteomics | Phosphorylation status of PCM proteins | Cell cycle regulation |
| Super-resolution microscopy | Sub-PCM localization of proteins | Structural studies |
Fluorescence microscopy and live-cell imaging
Immunofluorescence and live-cell imaging with fluorescently tagged PCM proteins are the primary methods to visualize protein localization to the pericentriolar material. Tagged knock-in cell lines expressing GFP- or mCherry-fused proteins allow dynamic tracking of PCM recruitment during the cell cycle [4,8]. High-resolution confocal or super-resolution microscopy can resolve substructures within the PCM.
Proteomics and interactomics
Mass spectrometry-based proteomics of isolated centrosomes or proximity-labeling (BioID) can identify proteins that localize to the PCM and their interaction partners [2,6]. These approaches have revealed that the PCM scaffold interacts with RNA-binding proteins and centriolar satellites [4,6].
CRISPR-based genetic screens
Genome-wide CRISPR knockout screens can identify genes required for PCM protein localization. Cells are subjected to imaging-based screens to detect mislocalization of a fluorescent PCM marker, and candidate genes are validated [3,7]. This approach is powerful for discovering novel regulators of GO:1905793.
RNA localization assays
RNA fluorescence in situ hybridization (FISH) and RNA-seq of centrosome-enriched fractions can detect RNAs localized to the PCM. The PCM scaffold enables RNA localization, and disrupting scaffold proteins abolishes this localization.
How CRISPR Can Be Used to Study GO:1905793 protein localization to pericentriolar material
Knockout
CRISPR knockout of genes encoding PCM proteins or their regulators is used to test their requirement for protein localization to the pericentriolar material. For example, knockout of Cep72 disrupts microtubule nucleation and spindle formation. Knockout of CPAP leads to centriole fragmentation and impaired PCM organization. These models are essential for loss-of-function studies.
Point Mutation
Point mutation knock-in allows researchers to test the function of specific amino acid residues, such as phosphorylation or acetylation sites, in PCM protein localization. A cell cycle-dependent transition from acetylation to phosphorylation regulates timely centrosome maturation, and point mutations that mimic or block these modifications can reveal their precise roles. This approach is also used to model disease-associated mutations in genes like CEP290.
Knock-in
Knock-in of tagged versions of PCM proteins (e.g., GFP, HaloTag) enables live-cell imaging of their localization and dynamics. Tagged knock-in of CCHCR1 has been used to study its centrosomal localization and interaction with OFD1 and PCM1. Knock-in of wild-type CPAP into CPAP-null cells can rescue centriole fragmentation.
Overexpression
Overexpression of PCM proteins or their regulators can drive centrosome amplification and disrupt normal localization. For example, overexpression of CDK5RAP2 or Aurora A leads to PCM overgrowth and mitotic defects [3,8]. Overexpression studies complement knockout approaches by revealing gain-of-function phenotypes.
How EDITGENE Supports protein localization to pericentriolar material Research
Researchers studying protein localization to pericentriolar material-related genes often need to determine whether a candidate gene is causally involved in PCM assembly, cell cycle progression, or disease. EDITGENE provides a comprehensive suite of CRISPR-based services to generate precisely engineered cell models, enabling rigorous functional validation of genes implicated in GO:1905793.
Contact EDITGENE today to design your custom CRISPR model for protein localization to pericentriolar material research.
Frequently Asked Questions About protein localization to pericentriolar material
What is GO:1905793?
GO:1905793 is a Gene Ontology biological process term defined as the process in which a protein is transported to, or maintained in, a location within a pericentriolar material.
What is protein localization to pericentriolar material?
It is the cellular process of delivering or retaining proteins within the pericentriolar material (PCM), the matrix surrounding centrioles that nucleates microtubules.
What genes are involved in protein localization to pericentriolar material?
Key genes include Cep72, CPAP, CDK5RAP2, CEP290, CCHCR1, PCM1, OFD1, WDR5, MLL, pericentrin, CEP192, and Spd-2 [1,2,5,6,7,8].
How is protein localization to the PCM regulated?
It is regulated by cell cycle-dependent phosphorylation and acetylation, CDK activity, and the MLL/WDR5 complex [2,3,8].
Why is protein localization to the pericentriolar material important?
It is essential for centrosome maturation, mitotic spindle assembly, chromosome segregation, and ciliogenesis [4,5,6,8].
What diseases are associated with defects in PCM protein localization?
Cancer, ciliopathies such as Joubert syndrome, and developmental disorders [1,5,6].
What methods are used to study protein localization to the PCM?
Immunofluorescence, live-cell imaging, proteomics, CRISPR screens, and RNA FISH [2,3,4,6].
Can CRISPR be used to study protein localization to the pericentriolar material?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression models are widely used to dissect gene function in this process [1,2,5,8].
What is the role of Cep72 in the PCM?
Cep72 is a centriolar satellite protein recruited to the PCM by the MLL/WDR5 complex, where it regulates microtubule nucleation and spindle formation.
How does the PCM scaffold enable RNA localization?
The PCM scaffold provides binding sites for RNA-binding proteins, allowing RNAs to be localized to centrosomes for local translation.
Conclusion
GO:1905793, protein localization to pericentriolar material, is a fundamental biological process that ensures the correct spatiotemporal assembly of the centrosomal matrix. It is regulated by cell cycle-dependent post-translational modifications and involves a diverse set of proteins including Cep72, CPAP, CDK5RAP2, CEP290, and CCHCR1 [1,2,3,5,6,8]. Defects in this process are linked to cancer, ciliopathies, and developmental disorders, making it a critical area of research [1,5,6]. Advances in CRISPR-based gene editing and imaging technologies continue to unravel the molecular mechanisms of PCM protein localization, offering new opportunities for therapeutic intervention [4,7].
References
- 1. Vásquez-Limeta A et al.. 2022. CPAP insufficiency leads to incomplete centrioles that duplicate but fragment.. J Cell Biol 221(5) PMID: 35404385
- 2. Chodisetty S et al.. 2024. MLL/WDR5 complex recruits centriolar satellite protein Cep72 to regulate microtubule nucleation and spindle formation.. Sci Adv 10(50):eadn0086 PMID: 39661677
- 3. Roberts EL et al.. 2024. CDK activity at the centrosome regulates the cell cycle.. Cell Rep 43(4):114066 PMID: 38578823
- 4. Fang J et al.. 2025. The PCM scaffold enables RNA localization to centrosomes.. Mol Biol Cell 36(6):ar75 PMID: 40305119
- 5. Matsuo K et al.. 2025. Focal adhesion-related non-ciliary functions of CEP290.. PLoS One 20(7):e0325921 PMID: 40632733
- 6. Zhang J et al.. 2025. CCHCR1 links P-body proteins to the centrosome and is required for ciliogenesis through interacting with OFD1 and PCM1.. Cell Mol Biol Lett 30(1):103 PMID: 40883668
- 7. O'Neill RS et al.. 2023. Spd-2 gene duplication reveals cell-type-specific pericentriolar material regulation.. Curr Biol 33(14):3031-3040.e6 PMID: 37379844
- 8. Li J et al.. 2026. A cell cycle-dependent transition of acetylation to phosphorylation regulates timely centrosome maturation.. Nat Commun 17(1) PMID: 41862458
