Depalmitoylation of CAAX motif proteins

Protein structural determinants of palmitate turnover rate

Jui Yun Lu, Sandra L. Hofmann

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

In the present study, we examined the effect of amino acid substitutions on the rate of turnover of palmitate bound to a model "CAAX" motif protein H-Ras. These experiments were designed to shed light on the specificity of the process that removes palmitate from prenylated proteins. H-Ras, protein A-Ras fusion constructs, and constructs with amino acid substitutions in the H-Ras hypervariable region were transfected into COS cells, and the turnover rate of palmitate bound to each expressed protein was measured. We found no evidence for strict sequence specificity for palmitate removal, but found a strong inverse correlation between palmitate turnover rate and the degree of membrane association for any given construct, with slower turnover rates associated with stronger membrane binding. These data support a model in which the palmitate turnover rate is determined by access to a depalmitoylating enzyme and argue against a more complex model in which specific recognition of palmitoylated proteins is required.

Original languageEnglish (US)
Pages (from-to)7251-7256
Number of pages6
JournalJournal of Biological Chemistry
Volume270
Issue number13
StatePublished - Mar 31 1995

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Amino Acid Motifs
Palmitates
ras Proteins
Proteins
Amino Acid Substitution
Substitution reactions
Membranes
Amino Acids
COS Cells
Staphylococcal Protein A
Fusion reactions
Association reactions
Enzymes
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

Depalmitoylation of CAAX motif proteins : Protein structural determinants of palmitate turnover rate. / Lu, Jui Yun; Hofmann, Sandra L.

In: Journal of Biological Chemistry, Vol. 270, No. 13, 31.03.1995, p. 7251-7256.

Research output: Contribution to journalArticle

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