QuickView for staurosporine (compound)

Tyrosine kinase that plays an essential role for the selection and maturation of developing T-cell in the thymus and in mature T-cell function. Is constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors and plays a key role in T-cell antigen receptor(TCR)-linked signal transduction pathways. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, and thereby recruits the associated LCK to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosines-based activation motifs (ITAMs) in the cytoplasmic tails of the TCRgamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. In addition, contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, and upon engagement of the CD2 molecule, LCK undergoes hyperphosphorylation and activation. Also plays a role in the IL2 receptor-linked signaling pathway that controls T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR

Plays a role in signal transduction in blood cells. Contributes to both cell proliferation and survival and thus provide a selective advantage in tumorigenesis. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3

Plays a role in T-cell proliferation and differentiation

Positive effector of BCR-stimulated responses. Couples the B-cell antigen receptor (BCR) to the mobilization of calcium ion either through a phosphoinositide 3-kinase-dependent pathway, when not phosphorylated on tyrosines of the linker region, or through a phospholipase C-gamma-dependent pathway, when phosphorylated on Tyr-348 and Tyr-352. Thus the differential phosphorylation of Syk can determine the pathway by which BCR is coupled to the regulation of intracellular calcium ion

Its physiological substrate seems to be the small heat shock protein (HSP27/HSP25). In vitro can phosphorylate glycogen synthase at 'Ser-7' and tyrosine hydroxylase (on 'Ser-19' and 'Ser-40'). This kinase phosphorylates Ser in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Mediates both ERK and p38 MAPK/MAPK14 dependent neutrophil responses. Participates in TNF alpha-stimulated exocytosis of secretory vesicles in neutrophils. Plays a role in phagocytosis-induced respiratory burst activity

Participates in the Wnt signaling pathway. Implicated in the hormonal control of several regulatory proteins including glycogen synthase, MYB and the transcription factor JUN. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA

Specifically phosphorylates 'Tyr-504' on LCK, which acts as a negative regulatory site. Can also act on the LYN and FYN kinases

Probably involved in the control of the cell cycle. Interacts with cyclins A, B3, D, or E. Activity of CDK2 is maximal during S phase and G2

3-phosphorylates the cellular phosphoinositide PtdIns- 4,5-biphosphate (PtdIns(4,5)P2) to produce PtdIns-3, 4,5- triiphosphate (PtdIns(3,4,5)P3). Links G-protein coupled receptor activation to the secondary messenger PtdIns(3,4,5)P3 production

Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling processes and in development. Isoform 3 is catalytically inactive

PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters

Associates with the T-cell antigen receptor zeta chain (CD3Z). Plays a role in lymphocyte activation

Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells