CDC42 was initially identified in the yeast Saccharomyces cerevisiae as a mediator of cell division . The human CDC42 protein consists of 191 amino acids and has a theoretical weight of approximately 21.33 kDa . It functions as a homodimer with A and B chains . The protein contains several important domains, including a P-loop containing nucleoside triphosphate hydrolase and a small GTP-binding protein domain .
CDC42 cycles between an active GTP-bound state and an inactive GDP-bound state . This cycling is regulated by three types of proteins:
Activated CDC42 induces conformational changes in p21-activated kinases (PAK1 and PAK2), which subsequently initiate actin reorganization and regulate cell adhesion, migration, and invasion .
Recent studies have shown that CDC42 actively contributes to cancer progression . It is overexpressed in various cancers, including non-small cell lung cancer, colorectal adenocarcinoma, melanoma, breast cancer, and testicular cancer . Elevated levels of CDC42 have been correlated with negative patient survival. The protein is required for both G1-S phase progression and mitosis and modulates transcription factors such as SRF, STAT3, and NFkB . Targeting CDC42 in conjunction with chemotherapy is being explored as a potential cancer treatment strategy .
CDC42 has been implicated in several diseases, including Takenouchi-Kosaki Syndrome and Neonatal-Onset Severe Multisystemic Autoinflammatory Disease with Increased IL18 . Its role in regulating actin polymerization through direct binding to Neural Wiskott-Aldrich syndrome protein (N-WASP) and subsequent activation of the Arp2/3 complex is crucial for various cellular processes .
Human recombinant CDC42 is widely used in research to study its role in cell signaling pathways and its implications in diseases. Understanding the molecular mechanisms of CDC42 can provide insights into developing targeted therapies for cancer and other diseases.