phospho-Mst2 (Thr180) Rabbit pAb (一抗) | Bioss

STK3

Serine/threonine-protein kinase 3

Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation. Interacts with and stabilizes SAV1. Interacts with RAF1, which prevents dimerization and phosphorylation. Interacts with RASSF1. Interacts (via SARAH domain) with isoform 1 of NEK2. Interacts with ESR1 only in the presence of SAV1. Interacts with PKB/AKT1. Forms a tripartite complex with MOBKL1B and STK38. Interacts with RASSF2 (via SARAH domain).

Cytoplasm. Nucleus. Note: The caspase cleaved form cycles between the nucleus and cytoplasm.

Expressed at high levels in adult kidney, skeletal and placenta tissues and at very low levels in adult heart, lung and brain tissues.

Phosphorylation at Thr-117 and Thr-384 by PKB/AKT1, leads to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation, and increase in its binding to RAF1.
Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N).

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.
Contains 1 protein kinase domain.
Contains 1 SARAH domain.

The human serine/threonine kinase, mammalian STE20 like kinase (MST), is considerably homologous to the budding yeast kinases, SPS1 and STE20, throughout their kinase domains. When stably expressed in HeLa cells, MST highly sensitizes the cells to death receptor mediated apoptosis by accelerating caspase 3 activation. These findings suggest that MST1 and MST2 play a role in apoptosis both upstream and downstream of caspase activation. MST1 is cleaved and activated by caspases during apoptosis and is capable of inducing apoptotic morphological changes such as chromatin condensation upon overexpression. Mammalian Sterile 20 Like 2 (MST2) is most similar to the previously identified MST1 protein kinase (78% identity, 88% similarity). Northern analysis indicates that MST2 mRNA is expressed at high levels in adult kidney, skeletal and placental tissues and at very low levels in adult heart, lung, liver and brain tissues. An in vitro kinase assay indicates that MST2 can phosphorylate an exogenous substrate, as well as itself, and phospho amino acid analysis indicates that it is a serine/threonine protein kinase.