Ca2+ influx and protein scaffolding via TRPC3 sustain PKCβ and ERK activation in B cells
Year: 2010
Type: article
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.
Source: Journal of Cell Science
DOI: 10.1242/jcs.061051
Language: English
Topic: Ion Channels and Receptors
Subfield: Sensory Systems
Field: Neuroscience
Domain: Life Sciences
Open Access status: green
Awards: Mechanisms of Generation, Maintenance, and Activation of Humoral Memory, Functional characterization of redox-sensitive ion channels usingchemical library, Molecular elucidation and medical significance of redox-sensitive TRP channels in inflammatory cell infiltration., Study on the role of receptor-activated cation channel TRPC3 in cardiac remodeling, On the mechanism of modal regulation of cardiovascular Ca2+entry channel TRPC6
OpenAlex ID: W2140922576