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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Phospholipase C-gamma is required for agonist-induced Ca2+ entry

Cited 139 times inthomson ciCited 143 times inthomson ci
Title
Phospholipase C-gamma is required for agonist-induced Ca2+ entry
Author
Patterson, RLvan Rossum, DBFord, DLHurt, KJBae, SSSuh, Pann-GhillKurosaki, TSnyder, SHGill, DL
Keywords
CAPACITATIVE CALCIUM-ENTRY; OPERATED HTRP3 CHANNELS; NECROTIC CELL-DEATH; TYROSINE PHOSPHORYLATION; ENDOPLASMIC-RETICULUM; STORE DEPLETION; TRPC3 CHANNELS; RECEPTOR; PROTEIN; ACTIVATION
Issue Date
200211
Publisher
CELL PRESS
Citation
CELL, v.111, no.4, pp.529 - 541
Abstract
We report here that PLC-γ isoforms are required for agonist-induced Ca2+ entry (ACE). Overexpressed wild-type PLC-γ1 or a lipase-inactive mutant PLC-γ1 each augmented ACE in PC12 cells, while a deletion mutant lacking the region containing the SH3 domain of PLC-γ1 was ineffective. RNA interference to deplete either PLC-γ1 or PLC-γ2 in PC12 and A7r5 cells inhibited ACE. In DT40 B lymphocytes expressing only PLC-γ2, overexpressed muscarinic M5 receptors (M5R) activated ACE. Using DT40 PLC-γ2 knockout cells, M5R stimulation of ER Ca2+ store release was unaffected, but ACE was abolished. Normal ACE was restored by transient expression of PLC-γ2 or a lipase-inactive PLC-γ2 mutant. The results indicate a lipase-independent role of PLC-γ in the physiological agonist-induced activation of Ca2+ entry.
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DOI
http://dx.doi.org/10.1016/S0092-8674(02)01045-0
ISSN
0092-8674
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