Phospholipase C-β3 and -β1 form homodimers, but not heterodimers, through catalytic and carboxyl-terminal domains

Yong Zhang, Walter K. Vogel, Jennifer S. McCullar, Jeffrey A. Greenwood, Theresa M. Filtz

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Phospholipase C-β (PLC-β) isoenzymes are key effectors in G protein-coupled signaling pathways. Prior research suggests that some isoforms of PLC-β may exist and function as dimers. Using coimmunoprecipitation assays of differentially tagged PLC-β constructs and size-exclusion chromatography of native PLC-β, we observed homodimerization of PLC-β3 and PLC-β1 isoenzymes but failed to detect heterodimerization of these isoenzymes. Size-exclusion chromatography data suggest that PLC-β3 and PLC-β1 form higher affinity homodimers than PLC-β2. Evidence supportive of limited PLC-β monomer-homodimer equilibrium appears at ≤100 nM. Further assessment of homodimerization status by coimmunoprecipitation assays with differentially tagged PLC-β3 fragments demonstrated that at least two subdomains of PLC-β3 are involved in dimer formation, one in the catalytic X and Y domains and the other in the G protein-regulated carboxyl-terminal domain. In addition, we provide evidence consistent with the existence of PLC-β homodimers in a whole-cell context, using fluorescent protein-tagged constructs and microscopic fluorescence resonance energy transfer assays.

Original languageEnglish (US)
Pages (from-to)860-868
Number of pages9
JournalMolecular Pharmacology
Issue number3
StatePublished - 2006
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmacology


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