Journal
JOURNAL OF CELL SCIENCE
Volume 123, Issue 6, Pages 927-938Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.061051
Keywords
B-cell receptor; Ca2+ signaling; Diacylglycerol; PKC beta; TRP channels
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Japan Society for the Promotion of Sciences
- NIH
- National Institute of Environmental Health Sciences
- Grants-in-Aid for Scientific Research [22681033, 20249015, 22689003, 21590246, 21229007] Funding Source: KAKEN
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Ca2+ 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 Ca2+ entry activated by Ins(1,4,5)P-3-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 C beta (PKC beta) that activated extracellular signal-regulated kinase (ERK). Notably, TRPC3 showed direct association with PKC beta that maintained localization of PKC beta at the PM. Thus, TRPC3 functions as both a Ca2+-permeable channel and a protein scaffold at the PM for downstream PKC beta activation in B cells.
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