CASK interacting protein 2 (CASKIN2)

CASK interacting protein 2 (CASKIN2) is a large, multidomain neuronal scaffold protein characterized by six ankyrin repeats, a Src homology 3 (SH3) domain, and two sterile alpha motif (SAM) domains, along with extended proline-rich and conserved C-terminal regions[1][2][3][4]. It plays a key role in organizing postsynaptic protein complexes and modulating synaptic plasticity by nucleating large macromolecular assemblies at synaptic sites[1][3]. Although highly homologous to CASKIN1, CASKIN2 lacks a direct CASK interaction domain, leading to unique signaling roles. CASKIN2 binds talin and Abi1, linking integrin-mediated adhesion to cytoskeletal reorganization and migration, particularly in the context of some tumors[2]. In the nervous system, knockout studies indicate essential functions in memory, recognition, dendritic spine morphology, and synaptic receptor phosphorylation[1]. CASKIN2 can polymerize via its SAM domains into dimeric repeat units, a property thought to allow dynamic macromolecular assembly and organization at signaling sites[3][4]. Currently, no drugs are known to modulate CASKIN2, nor is it used as a diagnostic biomarker.

Other names

ANKS5BCaskin-2KIAA1139FLJ21609CASKIN2caskin-2