Slingshot protein phosphatase 2 (SSH2)

Slingshot protein phosphatase 2 (SSH2) is a member of the protein phosphatase family essential for actin cytoskeleton regulation. SSH2 functions as an enzyme that dephosphorylates and activates the actin-binding protein cofilin, thereby promoting actin filament depolymerization. This is crucial for processes such as cell motility, cytoskeleton reorganization, and vesicular trafficking, especially during developmental events like spermatogenesis and acrosome biogenesis. SSH2 activity is controlled by auto-inhibition and is triggered in response to specific cellular signals, linking its enzymatic function to the state of the actin network[1][2][3][4][5]. Studies in knockout mice show SSH2 is indispensable for male fertility, with its loss causing impaired acrosome biogenesis and spermatogenesis arrest due to failed actin remodeling[2][3]. SSH2 has emerged as a potential therapeutic target in cancer and may play broader roles in other pathologies involving cytoskeletal dysfunction[1][3].

Other names

Slingshot phosphatase 2SSH2LSSH-2LhSSH-2LKIAA1725SSH-like protein 2SSH-2protein phosphatase Slingshot homolog 2

Inhibitors or modulators would regulate actin filament dynamics by altering cofilin activation through SSH2