Ca2+ influx and protein scaffolding via TRPC3 sustain PKCβ and ERK activation in B cells

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

研究成果: Contribution to journalArticle査読

56 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)927-938
ページ数12
ジャーナルJournal of cell science
123
6
DOI
出版ステータス出版済み - 3 15 2010

All Science Journal Classification (ASJC) codes

  • Cell Biology

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