Trafficking and signaling by fatty-acylated and prenylated proteins Journal Article


Author: Resh, M. D.
Article Title: Trafficking and signaling by fatty-acylated and prenylated proteins
Abstract: A wide variety of signaling proteins are modified by covalently linked fatty acids and/or prenyl groups. These hydrophobic moieties, which include myristate, palmitate, farnesyl and geranylgeranyl, are more than just fat: they provide distinct information that modulates the specificity and efficiency of signal transduction. Recent studies show that lipid modification influences the movement of a signaling protein within the cell and its final destination. Protein lipidation can also confer reversible association with membranes and other signaling proteins. These findings provide new insights into the biochemical and biophysical mechanisms that regulate membrane targeting, trafficking and signaling by lipid-modified proteins. © 2006 Nature Publishing Group.
Keywords: signal transduction; unclassified drug; review; binding affinity; proteins; animals; models, biological; protein protein interaction; protein targeting; protein; enzyme activity; abelson kinase; regulatory mechanism; protein transport; fatty acids; arf protein; endocytosis; fatty acid; membrane binding; chemical modification; cyclic amp dependent protein kinase; acylation; protein lipid interaction; palmitoylation; myristic acid; myristylation; gag protein; palmitic acid; prenylation; protein isoprenylation; clonal anergy; frequenin; hippocalcin; hisactophilin; marcks protein; neurocalcin; recoverin; visinin
Journal Title: Nature Chemical Biology
Volume: 2
Issue: 11
ISSN: 1552-4450
Publisher: Nature Publishing Group  
Date Published: 2006-11-01
Start Page: 584
End Page: 590
Language: English
DOI: 10.1038/nchembio834
PUBMED: 17051234
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 158" - "Export Date: 4 June 2012" - "Source: Scopus"
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  1. Marilyn D Resh
    120 Resh
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