BR serine/threonine Kinase 2 Proteins (BRSK2)

Human BR serine/threonine Kinase 2 (BRSK2) interaction partners

1. the intrinsic molecular merit that BRSK2 provides is a survival advantage to PDAC cells and strengthens the invasiveness of these neoplastic cells in energy-deprived environments.

2. SAD-A and AMPK kinases are regulators of mTORC1 signaling in the pancreatic beta-cells.

3. BRSK2 interacted with VCP/p97 via three of the four functional domains of VCP/p97. Immunofluorescence demonstrated that BRSK2 and VCP/p97 were co-localized and also that knockdown of endogenous BRSK2 induced increased levels of CD3delta.

4. Anaphase-promoting complex/cyclosome-Cdh1, rather than Cdc20, promotes the degradation of BRSK2 in vivo.

5. a novel function of BRSK2 in the regulation of GSIS in beta-cells via a PCTAIRE1-dependent mechanism and suggest that BRSK2 is an attractive target for developing novel diabetic drugs.

6. these findings demonstrate ER stress may reduce BRSK2 protein and change BRSK2 subcellular localization, which in turn alleviate ER stress-induced apoptosis.

7. these findings provide a novel regulatory mechanism of BRSK2 through direct interaction with Jab1.

8. BRSK2 is up-regulated in pancreatic ductal adenocarcinoma.

9. BRSK2 may be an autoantigen involved in the pathogenesis of small-cell lung cancer-associated limbic encephalitis.

10. we identified cAMP-dependent protein kinase A (PKA) as another upstream kinase of BRSK2, which can phosphorylate BRSK2 at Thr260. Kinase activity of BRSK2 can be increased through phosphorylation by PKA.

11. protein phosphatase 2C is a likely candidate for catalyzing the dephosphorylation and inactivation of BRSK1/2.

12. level of SAD within neurons is modulated by TORC1

13. STRADalpha.MO25alpha complexes containing LKB1 variants were equally effective at phosphorylating and activating AMPK, BRSK1, and BRSK2

Mouse (Murine) BR serine/threonine Kinase 2 (BRSK2) interaction partners

1. Glucose and incretin stimulate insulin secretion through the phosphorylation of GDIalpha at Ser174 by SAD-A, which leads to the activation of Rho GTPases, culminating in insulin exocytosis.

2. Taken together, these data suggest a model for synergistic autoinhibition and membrane activation of SAD kinases.

3. SAD-A and AMPK kinases are regulators of mTORC1 signaling in the pancreatic beta-cells.

4. SAD-A and SAD-B kinases have multiple, sequential roles in axonal differentiation

5. SAD-A kinase controls islet beta-cell size and function as a mediator of mTORC1 signaling.

6. SAD-A kinase is a pancreas-specific mediator of incretin response in islet beta cells.

7. a novel function of BRSK2 in the regulation of GSIS in beta-cells via a PCTAIRE1-dependent mechanism and suggest that BRSK2 is an attractive target for developing novel diabetic drugs.

8. a critical role of SAD-A in the activation of PAK1 during the onset of insulin exocytosis.

9. The regulation of Wee1 by SadA and SadB kinases is essential for the differentiation of polarized neurons.

10. results show that SAD-A and SAD-B, mammalian orthologs of a kinase needed for presynaptic differentiation in Caenorhabditis elegans, are required for neuronal polarization.

11. Once activated, LKB1 phosphorylates and thereby activates SAD-A and SAD-B kinases, which are also required for neuronal polarization in the cerebral cortex.