Analysis of TRPC3-interacting proteins by tandem mass spectrometry

Journal of Proteome Research
Timothy P LockwichIndu S Ambudkar

Abstract

Mammalian transient receptor potential canonical (TRPC) channels are a family of nonspecific cation channels that are activated in response to stimulation of phospholipase C (PLC)-dependent hydrolysis of the membrane lipid phosphatidylinositol 4,5-bisphosphate. Despite extensive studies, the mechanism(s) involved in regulation of mammalian TRPC channels remains unknown. Presence of various protein-interacting domains in TRPC channels have led to the suggestion that they associate with proteins that are involved in their function and regulation. This study was directed toward identifying the proteins associated with native TRPC3 using a shotgun proteomic approach. Anti-TRPC3 antibody was used to immunoprecipitate TRPC3 from solubilized rat brain crude membranes under conditions that allow retention of TRPC3 function. Proteins in the TRPC3 (using anti-TRPC3 antibody) and control (using rabbit IgG) immunoprecipitates were separated by SDS-PAGE, the gel was sectioned, and the resolved proteins were digested by trypsin in situ. After extraction of the peptides, the peptides were separated by HPLC and sequences derived by MS/MS. Analysis of the data revealed 64 specific TRPC3-associated proteins which can be grouped in terms of their...Continue Reading

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Citations

Jun 19, 2013·Proceedings of the National Academy of Sciences of the United States of America·Shengjie FengYizheng Wang
May 17, 2013·Pflügers Archiv : European journal of physiology·Jung Nyeo ChunJu-Hong Jeon
Jul 12, 2014·Cell Calcium·Lorena Brito de Souza, Indu S Ambudkar
Mar 29, 2011·Cold Spring Harbor Perspectives in Biology·Jana HartmannArthur Konnerth
Apr 30, 2015·Cell Calcium·Hwei Ling Ong, Indu S Ambudkar
Jul 13, 2011·Channels·Hwei Ling Ong, Indu S Ambudkar
Mar 30, 2010·Biochimica Et Biophysica Acta·Sylvie CayouetteGuylain Boulay

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