Testis-associated actin remodelling kinase 1 (TESK1)

Testis-associated actin remodelling kinase 1 (TESK1) is a serine/threonine protein kinase with dual specificity, containing an N-terminal kinase domain and a C-terminal proline-rich domain[1][2][3]. It is structurally related to the LIM kinase subclass of kinases. TESK1 was originally identified in the testis and is highly expressed in testicular tissue, but also found at lower levels in other tissues, such as the brain[2][3]. Its primary function is the phosphorylation of cofilin on Serine-3, leading to inactivation of cofilin and thereby promoting actin stress fiber formation and stabilization of the actin cytoskeleton[1][2][3]. TESK1 activity is stimulated by integrin signaling, linking it to extracellular matrix interactions and cell adhesion[1]. It also participates in the regulation of cell spreading and motility and is implicated in various developmental processes. TESK1 interacts with proteins such as Spred1 and Sprouty4, which can inhibit its kinase activity[2]. Disease associations primarily involve male infertility (spermatogenic failure) and possible links to neurodegeneration in model organisms[3][2]. No currently approved drugs are known to selectively target TESK1 in the clinic, and its direct use as a biomarker or drug target is investigational.

Other names

Dual specificity testis-specific protein kinase 1Testicular protein kinase 1Testis-specific kinase 1TESK1