Referenced in: none

Automatically associated channels: Slo1

Title: Ca2+ influx and protein scaffolding via TRPC3 sustain PKCbeta and ERK activation in B cells.

Authors: Takuro Numaga, Motohiro Nishida, Shigeki Kiyonaka, Kenta Kato, Masahiro Katano, Emiko Mori, Tomohiro Kurosaki, Ryuji Inoue, Masaki Hikida, James W Putney, Yasuo Mori

Journal, date & volume: J. Cell. Sci., 2010 Mar 15 , 123, 927-38

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/20179100

Abstract
Ca(2+) signaling mediated by phospholipase C that produces inositol 1,4,5-trisphosphate [Ins(1,4,5)P(3)] and diacylglycerol (DAG) controls lymphocyte activation. In contrast to store-operated Ca(2+) entry activated by Ins(1,4,5)P(3)-induced Ca(2+) release from endoplasmic reticulum, the importance of DAG-activated Ca(2+) entry remains elusive. Here, we describe the physiological role of DAG-activated Ca(2+) entry channels in B-cell receptor (BCR) signaling. In avian DT40 B cells, deficiency of transient receptor potential TRPC3 at the plasma membrane (PM) impaired DAG-activated cation currents and, upon BCR stimulation, the sustained translocation to the PM of protein kinase Cbeta (PKCbeta) that activated extracellular signal-regulated kinase (ERK). Notably, TRPC3 showed direct association with PKCbeta that maintained localization of PKCbeta at the PM. Thus, TRPC3 functions as both a Ca(2+)-permeable channel and a protein scaffold at the PM for downstream PKCbeta activation in B cells.