Phospholipase C-γ: Diverse roles in receptor-mediated calcium signaling

Randen L. Patterson, Damian B. Van Rossum, Nikolas Nikolaidis, Donald L. Gill, Solomon H. Snyder

Research output: Contribution to journalReview articlepeer-review

100 Scopus citations


Ca2+ is a universal signal: the dynamic changes in its release and entry trigger a plethora of cellular responses. Central to this schema are members of the phospholipase C (PLC) superfamily, which relay information from the activated receptor to downstream signal cascades by production of second-messenger molecules. Recent studies reveal that, in addition to its enzymatic activity, PLC-γ regulates Ca2+ entry via the formation of an intermolecular lipid-binding domain with canonical transient receptor potential 3 (TRPC3) ion channels. This complex, in turn, controls TRPC3 trafficking and cell-surface expression. Thus, TRPC3 ion channels are functionally linked to both lipase-dependent and -independent activities of PLC-γ. Understanding the underlying molecular mechanisms that regulate this complex will probably clarify the processes of receptor-activated Ca 2+ entry.

Original languageEnglish (US)
Pages (from-to)688-697
Number of pages10
JournalTrends in Biochemical Sciences
Issue number12
StatePublished - Dec 2005

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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