Anti-BRSK1

The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. BRSK1 (BR serine/threonine-protein kinase 1), also known as SAD1, is a 794 amino acid protein that localizes to both the nucleus and the cytoplasm and contains one UBA domain and one protein kinase domain. Expressed in a variety of tissues with highest expression in testis and brain, BRSK1 uses magensium as a cofactor to catalyze the ATP-dependent phosphorylation of target proteins, including Wee 1 and Cdc25B. Via its kinase activity toward proteins that are involved in microtubule assembly, BRSK1 plays an essential role in neuronal polarization and may be involved in regulating cell cycle arrest in response to DNA damage, Two isoforms of BRSK1 exist due to alternative splicing events. Protein function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C. [The UniProt Consortium]