Sorbin and SH3 domain-containing protein 3 (SORBS3)

Sorbin and SH3 domain-containing protein 3 (commonly known as Vinexin and abbreviated as SORBS3) is a cytoskeletal adaptor protein composed of multiple isoforms, including vinexin-alpha and vinexin-beta, which contain characteristic SH3 (Src homology 3) domains critical for protein–protein interactions[1][2]. It plays a key role in mechanotransduction by regulating the composition and dynamics of focal adhesions and actin cytoskeleton, notably through direct or indirect interactions with proteins such as vinculin and paxillin at sites of cell–extracellular matrix contacts[2][4]. SORBS3 modulates cell spreading, migration, and cellular responses to extracellular matrix stiffness, and it has been shown to negatively regulate autophagy in neurons, with expression levels rising during brain aging[3]. Knockout mouse models for SORBS3 reveal roles in cutaneous wound healing and sensitivity to cardiac hypertrophy, highlighting its functional importance in tissue repair and cardiovascular biology[2][3]. SORBS3 is not generally considered a therapeutic target for drug intervention at this time and no direct pharmacological modulators are documented in current literature.

Other names

VinexinSCAM1SCAM-1SH3D4SH3-containing adapter molecule 1Sorbin and SH3 domain containing 3vinexin beta (SH3-containing adaptor molecule-1)