西亚试剂：Sites of Regulated Phosphorylation that Control K-Cl Cotran

Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity

Jesse Rinehart1,5,Yelena D. Maksimova2,Jessica E. Tanis3,Kathryn L. Stone5,6,Caleb A. Hodson1,Junhui Zhang1,Mary Risinger7,Weijun Pan4,Dianqing Wu4,Christopher M. Colangelo5,6,Biff Forbush3,Clinton H. Joiner7,Erol E. Gulcicek5,6,Patrick G. Gallagher2andRichard P. Lifton1,5,,

1 Department of Genetics, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA
2 Department of Pediatrics, Yale University School of Medicine, New Haven, CT 06510, USA
3 Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510, USA
4 Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06510, USA
5 Yale/National Heart, Lung, and Blood Institute Proteomics Center, Yale University, New Haven, CT 06511, USA
6 Keck Biotechnology Resource Laboratory, Yale University, New Haven, CT 06511, USA
7 Cincinnati Comprehensive Sickle Cell Center, Division of Hematology/Oncology, University of Cincinnati College of Medicine and Department of Pediatrics, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229, USA

Modulation of intracellular chloride concentration ([Cl]i) plays a fundamental role in cell volume regulation and neuronal response to GABA. Cl exit via K-Cl cotransporters (KCCs) is a major determinant of [Cl]I; however, mechanisms governing KCC activities are poorly understood. We identified two sites in KCC3 that are rapidly dephosphorylated in hypotonic conditions in cultured cells and human red blood cells in parallel with increased transport activity. Alanine substitutions at these sites result in constitutively active cotransport. These sites are highly phosphorylated in plasma membrane KCC3 in isotonic conditions, suggesting that dephosphorylation increases KCC3's intrinsic transport activity. Reduction of WNK1 expression via RNA interference reduces phosphorylation at these sites. Homologous sites are phosphorylated in all human KCCs. KCC2 is partially phosphorylated in neonatal mouse brain and dephosphorylated in parallel with KCC2 activation. These findings provide insight into regulation of [Cl]i and have implications for control of cell volume and neuronal function.

• 以上资料由西亚试剂：http://www.xiyashiji.com/ 提供此产品的详细信息如密度,含量,分子式,分子量等均可在西亚官网查询   
• 相关产品如汞乙酸汞氯化汞氧化汞碘化汞硫酸汞硝酸汞溴化汞硝酸亚汞氯化亚汞乙酸苯汞碘化汞钾硫氰酸汞氯化氨基汞三氯生三氯氧磷三氯乙烯水合氯醛三氯化磷三氯化钌三氯化钛三氯化铱三氯化铑三氯硫磷三氯乙烷三氯甲烷三氯卡班TCC1,3,5-三氯苯1,2,4-三氯苯1,2,3-三氯苯无水氯化铝三氯乙酸酐三氯乙酸钠碘甲烷二碘甲烷三碘甲烷 三氟碘甲烷硫酸二甲酯氯磺酸苯硫酚苯硫酚钠3-氨基苯硫酚2,6-二氯苯硫酚2,4-二氯苯硫酚2,5-二氯苯硫酚2-甲氧基苯硫酚2-氯乙醇 等均有销售.欢迎订购