Persistent membrane association of activated and depalmitoylated G protein α subunits

C. Huang, J. A. Duncan, A. G. Gilman, S. M. Mumby

Research output: Contribution to journalArticle

81 Scopus citations

Abstract

Heterotrimeric signal-transducing G proteins are organized at the inner surface of the plasma membrane, where they are positioned to interact with membrane-spanning receptors and appropriate effectors. G proteins are activated when they bind GTP and inactivated when they hydrolyze the nucleotide to GDP. However, the topological fate of activated G protein α subunits is disputed. One model declares that depalmitoylation of α, which accompanies activation by a receptor, promotes release of the protein into the cytoplasm. Our data suggest that activation of G protein α subunits causes them to concentrate in subdomains of the plasma membrane but not to be released from the membrane. Furthermore, α subunits remained bound to the membrane when they were activated with guanosine 5′-(3-O-thio)triphosphate and depalmitoylated with an acyl protein thioesterase. Limitation of α subunits to the plasma membrane obviously restricts their mobility and may contribute to the efficiency and specificity of signaling.

Original languageEnglish (US)
Pages (from-to)412-417
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number2
DOIs
StatePublished - Jan 19 1999

Keywords

  • Immunofluorescence
  • Localization
  • Signal transduction
  • Thioesterase

ASJC Scopus subject areas

  • General

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