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Volume 272, Number 40, Issue of October 3, 1997 pp. 25360-25366
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The Coiled-coil Region of the G Protein  Subunit
MUTATIONAL ANALYSIS OF G AND EFFECTOR INTERACTIONS

(Received for publication, July 1, 1997)

From the Metabolic Diseases Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892

The  and  subunits of the heterotrimeric G proteins remain tightly associated throughout the signaling cycle as the dimer interacts with G, receptors, and effectors. A coiled-coil structure involving -helical segments at the N termini of the  and  subunits contributes to the dimerization interface and has been implicated in effector signaling in yeast. Scanning mutagenesis of the coiled-coil region of the mammalian ₁ subunit was performed to examine the effect of point mutations on assembly and effector signaling in COS cell cotransfection assays. In addition to the E10K mutation described previously, mutations A11E, L14E, and I18E in ₁ were found to block association, as evidenced by the failure of the G mutants to undergo cytosolic translocation with cotransfected nonisoprenylated G. Although none of 14 ₁ point mutations prevented the -dependent activation of the c-Jun N-terminal kinase (JNK) effector pathway, the D20K point mutation enhanced JNK but not phospholipase C-2 activation. These findings implicate the coiled-coil region of G in JNK signaling, provide further evidence that the structural features of the complex mediating effector regulation may differ among effectors, and identify single codons in the mammalian  subunit where mutation might yield a phenotype of defective signal transduction.

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