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.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Numaga T,Nishida M,Kiyonaka S,Kato K,Katano M,Mori E,Kurosaki T,Inoue R,Hikida M,Putney JW Jr,Mori Ydoi
10.1242/jcs.061051subject
Has Abstractpub_date
2010-03-15 00:00:00pages
927-38issue
Pt 6eissn
0021-9533issn
1477-9137pii
jcs.061051journal_volume
123pub_type
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