Trafficking and signaling by fatty-acylated and prenylated proteins.
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.
Resh
Marilyn D
MD
Cell Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Ave, Box 143, New York, New York 10021, USA. m-resh@ski.mskcc.org
D000215:Acylation; D000818:Animals; D005227:Fatty Acids / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D017368:Protein Prenylation; D021381:Protein Transport / Q000502:physiology; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
D005227:Fatty Acids; D011506:Proteins