Cellular morphology, adhesion, and motility occur through dynamic reorganization of actin-based superstructures. Actin-binding proteins are critical for regulating actin polymerization and superstructure formation. The Arp2/3 complex is an actin polymerization-inducing complex that includes Arp2, Arp3, p41-Arc, p34-Arc, p21-Arc, p20 Arc, and p16-Arc. Several actin binding proteins, WASP, cortactin, and Abp1, regulate the activity of the Arp2/3 complex. Abp1 (SH3P7, HIP-55) is the mammalian homologue of the yeast Abp1p, which has been shown to bind actin and to have roles in endocytosis. Abp1 contains a C-terminal Src homology 3 domain and an N-terminal actin depolymerization factor (ADF-H/C) domain that is homologous to a similar domain found in the actin severing protein, cofilin. Abp1 can bind Src kinases, hematopoietic progenitor kinase 1 (HPK-1), myosin I heavy chain kinase, and dynamin. Thus, Abp1 may be important for regulation of the actin cytoskeleton through its ability to interact with F-actin and various other cytoskeletal and cell signaling proteins.

References

*For more information, see UniProt Accession Q9UJU6

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