Open AccessCa2+ influx and protein scaffolding via TRPC3 sustain PKCβ and ERK activation in B cells
Author(s) -
Takuro Numaga,
Motohiro Nishida,
Shigeki Kiyonaka,
Kenta Kato,
Masahiro Katano,
Etsuro Mori,
Tomohiro Kurosaki,
Ryuji Inoue,
Masaki Hara,
James W. Putney,
Yasuo Mori
Publication year - 2010
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.061051
Subject(s) - trpc3 , diacylglycerol kinase , protein kinase c , biology , microbiology and biotechnology , endoplasmic reticulum , signal transduction , phospholipase c , mapk/erk pathway , protein kinase a , transient receptor potential channel , receptor , kinase , biochemistry , trpc
Ca2+ signaling mediated by phospholipase C that produces inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] and diacylglycerol (DAG) controls lymphocyte activation. In contrast to store-operated Ca2+ entry activated by Ins(1,4,5)P3-induced Ca2+ release from endoplasmic reticulum, the importance of DAG-activated Ca2+ entry remains elusive. Here, we describe the physiological role of DAG-activated Ca2+ 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 Cβ (PKCβ) that activated extracellular signal-regulated kinase (ERK). Notably, TRPC3 showed direct association with PKCβ that maintained localization of PKCβ at the PM. Thus, TRPC3 functions as both a Ca2+-permeable channel and a protein scaffold at the PM for downstream PKCβ activation in B cells.