SSH2
SSH2 (slingshot protein phosphatase 2, also known as KIAA1725) is a protein phosphatase that regulates actin filament dynamics. It dephosphorylates and activates the actin-depolymerising factor cofilin, promoting filament disassembly. Browse Assay Genie's current range of SSH2 research reagents below, or read on for the biology behind the target.
SSH2 is a protein phosphatase that controls the turnover of actin filaments. It removes the inhibitory phosphate from the actin-binding and depolymerising factor cofilin. Dephosphorylated cofilin is active, binds actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, and the source annotation notes that SSH2 may also dephosphorylate and inactivate LIMK1, so the enzyme may act on both sides of this regulatory switch.
The SSH2 gene encodes a protein tyrosine phosphatase and the protein belongs to the protein-tyrosine phosphatase family. It is listed with the EC numbers 3.1.3.16 and 3.1.3.48 and sits in the HGNC gene group of slingshot protein phosphatases, alongside SSH1 and SSH3. Alternative splicing of the SSH2 gene results in multiple transcript variants. The protein is annotated in the cytoplasm, the cytoskeleton, focal adhesions and the acrosome, a secretory vesicle of sperm cells. A mouse ortholog, Ssh2, is recorded.
SSH2 is required for spermatogenesis. It is involved in acrosome biogenesis, probably by regulating cofilin-mediated remodelling of the actin cytoskeleton during proacrosomal vesicle fusion and/or Golgi to perinuclear vesicle trafficking. The gene was previously named slingshot homolog 2 (Drosophila), reflecting its relationship to the Drosophila slingshot phosphatase.
SSH2 activates cofilin by dephosphorylation, making it a key enzyme for studying how actin filament disassembly is regulated.
Cofilin is inhibited by LIMK1 phosphorylation, and SSH2 may also dephosphorylate and inactivate LIMK1, which makes it relevant to this regulatory axis.
SSH2 is required for spermatogenesis, so it is a target for work on male germ cell development.
SSH2 is involved in acrosome formation, probably through cofilin-mediated actin remodelling during proacrosomal vesicle fusion and Golgi vesicle trafficking.
SSH2 is a protein phosphatase that regulates actin filament dynamics. It dephosphorylates and activates cofilin, which then binds actin filaments and stimulates their disassembly. It may also dephosphorylate and inactivate LIMK1, the kinase that phosphorylates cofilin. It is required for spermatogenesis.
SSH2 stands for slingshot protein phosphatase 2. UniProt names it protein phosphatase Slingshot homolog 2. Other designations are KIAA1725 and the earlier name slingshot homolog 2 (Drosophila). Alternative splicing gives multiple transcript variants of the SSH2 gene.
A mouse ortholog, Ssh2, is recorded. SSH2 belongs to the protein-tyrosine phosphatase family and to the slingshot protein phosphatase gene group, which also includes SSH1 and SSH3. Check the datasheet of any product for its validated reactivity.
Other slingshot protein phosphatases that share the cofilin-regulating function of SSH2.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q76I76; product specifications from Assay Genie datasheets.