CDC42BPA

CDC42BPA (CDC42 Binding Protein Kinase Alpha) is a Protein Coding gene. Diseases associated with CDC42BPA include Myotonic Dystrophy. Among its related pathways are Actin Nucleation by ARP-WASP Complex and G-protein signaling RAC1 in cellular process. Gene Ontology (GO) annotations related to this gene include identical protein binding and protein kinase activity. An important paralog of this gene is CDC42BPB.

Full Name

CDC42 Binding Protein Kinase Alpha

Function

Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration (PubMed:15723050, PubMed:9418861, PubMed:9092543).
Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715).
In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160).
Phosphorylates: PPP1R12A, LIMK1 and LIMK2 (PubMed:11340065, PubMed:11399775).
May play a role in TFRC-mediated iron uptake (PubMed:20188707).
In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity).
Triggers the formation of an extrusion apical actin ring required for epithelial extrusion of apoptotic cells (PubMed:29162624).

Biological Process

Actin cytoskeleton reorganization Source: UniProtKB
Actomyosin structure organization Source: UniProtKB
Cell migration Source: UniProtKB
Intracellular signal transduction Source: InterPro
Peptidyl-threonine phosphorylation Source: GO_Central
Protein phosphorylation Source: UniProtKB

Cellular Location

Cytoplasm; Lamellipodium. Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent. Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner.

PTM

Proteolytically cleaved by caspases upon apoptosis induction. The cleavage at Asp-478 by CASP3 increases its kinase activity (in vitro).