{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen XY"],"funding":["NIDDK NIH HHS","NHLBI NIH HHS","NCI NIH HHS"],"pagination":["30368-75"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3436288"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["287(36)"],"pubmed_abstract":["Brain-selective kinase 2 (BRSK2) has been shown to play an essential role in neuronal polarization. In the present study, we show that BRSK2 is also abundantly expressed in pancreatic islets and MIN6 β-cell line. Yeast two-hybrid screening, GST fusion protein pull-down, and co-immunoprecipitation assays reveal that BRSK2 interacts with CDK-related protein kinase PCTAIRE1, a kinase involved in neurite outgrowth and neurotransmitter release. In MIN6 cells, BRSK2 co-localizes with PCTAIRE1 in the cytoplasm and phosphorylates one of its serine residues, Ser-12. Phosphorylation of PCTAIRE1 by BRSK2 reduces glucose-stimulated insulin secretion (GSIS) in MIN6 cells. Conversely, knockdown of BRSK2 by siRNA increases serum insulin levels in mice. Our results reveal a novel function of BRSK2 in the "],"journal":["The Journal of biological chemistry"],"pubmed_title":["Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic β-cells."],"pmcid":["PMC3436288"],"funding_grant_id":["R01 DK083850","R01 DK054254","R01DK054254","CA124982","R01 CA124982","P30 DK020572","R01DK083850","R01 HL112248"],"pubmed_authors":["Liu JO","Yu L","Li J","Chen XY","Wang YF","Saiyin H","Gu XT","Zhang YJ","Wan B","Wang YL","Gao R","Ding HF","Dong WP","Najjar SM","Zhang CY"],"additional_accession":[]},"is_claimable":false,"name":"Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic β-cells.","description":"Brain-selective kinase 2 (BRSK2) has been shown to play an essential role in neuronal polarization. In the present study, we show that BRSK2 is also abundantly expressed in pancreatic islets and MIN6 β-cell line. Yeast two-hybrid screening, GST fusion protein pull-down, and co-immunoprecipitation assays reveal that BRSK2 interacts with CDK-related protein kinase PCTAIRE1, a kinase involved in neurite outgrowth and neurotransmitter release. In MIN6 cells, BRSK2 co-localizes with PCTAIRE1 in the cytoplasm and phosphorylates one of its serine residues, Ser-12. Phosphorylation of PCTAIRE1 by BRSK2 reduces glucose-stimulated insulin secretion (GSIS) in MIN6 cells. Conversely, knockdown of BRSK2 by siRNA increases serum insulin levels in mice. Our results reveal a novel function of BRSK2 in the ","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Aug","modification":"2025-04-18T18:26:38.411Z","creation":"2019-03-27T00:57:41Z"},"accession":"S-EPMC3436288","cross_references":{"pubmed":["22798068"],"doi":["10.1074/jbc.m112.375618","10.1074/jbc.M112.375618"]}}