The membrane localization of the G protein αs subunit is not dependent on its tenir sequence or effector domain

Michael Y. Degtyarev, Allen M. Spiegel, Teresa L.Z. Jones

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


The Gs protein subunit (αs) sequences conserved in non-myristoylated α subunits (TENIR, residues 369-373) or critical for adenylyl cyclase interaction were investigated as possible sites required for membrane localization. Substitutions were created by site-directed mutagenesis in which the TENIR residues were deleted from αs or added to the soluble, non-myristoylated αil. After transfection, COS cells were separated by centrifugation into particulate and soluble fractions. Immunoblots showed that these substitutions did not change the localization: αs ± TENIR in the particulate fraction, non-myristoylated αil ± TENIR in the soluble fraction. The constitutively active αis chimera (CH4A), containing four regions of αs sufficient for adenylyl cyclase activation, was mutated to prevent myristoylation (GA-CH4A). Immunoblots of transfected COS cell fractions showed CH4A in the particulate and GA-CH4A in the soluble fraction. While these regions did not lead to memebrane localization, the soluble GA-CH4A could activate adenylyl cyclase in the intact cell and after reconstitution with cyc- membranes.

Original languageEnglish (US)
Pages (from-to)25-33
Number of pages9
JournalCellular Signalling
Issue number1
StatePublished - Jan 1994
Externally publishedYes


  • COS cell transfection
  • G protein
  • adenylyl cyclase
  • membrane attachment
  • protein domains
  • protein targeting
  • site-directed mutagenesis

ASJC Scopus subject areas

  • Cell Biology


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