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Phospholipase C-3 and -1 Form Homodimers, but Not Heterodimers, through Catalytic and Carboxyl-Terminal Domains

Department of Pharmaceutical Sciences, College of Pharmacy (W.K.V., T.M.F.), Department of Biochemistry and Biophysics (J.A.G., T.M.F.), and the Molecular and Cellular Biology Program (Y.Z., J.S.M., T.M.F.), Oregon State University, Corvallis, Oregon

Phospholipase C- (PLC-) isoenzymes are key effectors in G protein-coupled signaling pathways. Prior research suggests that some isoforms of PLC- may exist and function as dimers. Using coimmunoprecipitation assays of differentially tagged PLC- constructs and size-exclusion chromatography of native PLC-, we observed homodimerization of PLC-3 and PLC-1 isoenzymes but failed to detect heterodimerization of these isoenzymes. Size-exclusion chromatography data suggest that PLC-3 and PLC-1 form higher affinity homodimers than PLC-2. Evidence supportive of limited PLC- monomer-homodimer equilibrium appears at 100 nM. Further assessment of homodimerization status by coimmunoprecipitation assays with differentially tagged PLC-3 fragments demonstrated that at least two subdomains of PLC-3 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- homodimers in a whole-cell context, using fluorescent protein-tagged constructs and microscopic fluorescence resonance energy transfer assays.

Received for publication December 28, 2005.

Accepted for publication June 8, 2006.

Address correspondence to: Theresa M. Filtz, 203 Pharmacy Building, Oregon State University, Corvallis, OR 97331-3507. E-mail: theresa.filtz{at}oregonstate.edu

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