GO:0097122 cyclin A2-CDK1 complex

The cyclin A2-CDK1 complex (GO:0097122) is a cellular component defined as a protein complex consisting of cyclin A2 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle, and cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. This complex is therefore a key node in the regulation of cell cycle progression. Researchers study GO:0097122 to understand how cyclin A2 and CDK1 cooperate to phosphorylate substrates that control cell division. The complex has been linked to phosphorylation of the CDK inhibitor p27, providing a direct mechanism by which it influences cell cycle progression. Because aberrant cell cycle control is a hallmark of cancer, the cyclin A2-CDK1 complex is a subject of ongoing investigation in oncology and molecular cell biology. This article summarizes the definition, composition, mechanism, and research methods relevant to GO:0097122, based on published literature.

GO:0097122 (cyclin A2-CDK1 complex) is a cellular component term describing a protein complex composed of cyclin A2 and cyclin-dependent kinase 1 (CDK1). Cyclin A2 acts as the regulatory subunit, while CDK1 is the catalytic subunit that becomes active upon binding to cyclin A2. The complex is a serine/threonine protein kinase complex that participates in cell cycle regulation.

The cyclin A2-CDK1 complex is important because it represents a direct molecular link between cyclin periodicity and CDK1 kinase activity, which is essential for orderly cell cycle progression. Its ability to phosphorylate substrates such as p27 places it at the center of cell cycle control mechanisms. Dysregulation of this complex can contribute to uncontrolled proliferation, making it relevant to cancer research and therapeutic targeting.

The following genes and proteins are directly or functionally associated with the cyclin A2-CDK1 complex (GO:0097122) based on published literature.

The cyclin A2-CDK1 complex is regulated by the availability of cyclin A2, which is periodic throughout the cell cycle, and by phosphorylation of CDK1. Myc stimulates cell cycle progression through activation of Cdk1 and phosphorylation of p27, indicating that upstream oncogenic signals can influence CDK1 activity.

Dysregulation of cyclin A2-CDK1 complex activity can contribute to uncontrolled cell proliferation, a hallmark of cancer. Myc-driven cell cycle progression via Cdk1 activation and p27 phosphorylation highlights a mechanism by which this complex may support tumor growth.

Because the cyclin A2-CDK1 complex phosphorylates p27, a CDK inhibitor, its activity can influence checkpoint control and genomic stability. Loss of proper regulation may lead to inappropriate cell cycle progression.

Co-immunoprecipitation followed by western blotting can detect the physical interaction between cyclin A2 and CDK1, confirming assembly of the complex.

In vitro kinase assays using immunopurified cyclin A2-CDK1 complex can measure phosphorylation of substrates such as p27.

CRISPR knockout screens can identify genes required for cyclin A2-CDK1 complex function and cell cycle progression.

RNA-seq and mass spectrometry-based proteomics can reveal changes in gene expression and protein phosphorylation associated with cyclin A2-CDK1 activity.

Researchers studying cyclin A2-CDK1 complex-related genes often need to determine whether a candidate gene is causally involved in cell cycle regulation or disease. EDITGENE provides CRISPR-based cell model services to enable such functional studies.

The cyclin A2-CDK1 complex (GO:0097122) is a central regulator of cell cycle progression, composed of cyclin A2 and CDK1. Its ability to phosphorylate substrates such as p27 links it to proliferative signaling and cancer. Continued research using CRISPR-based models will further elucidate its roles and therapeutic potential.