The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions

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• 作者：McLaughlin ; Stuart ; Aderem ; Alan
• 刊名：Trends in Biochemical Sciences
• 出版年：1995
• 出版时间：July, 1995
• 年：1995
• 卷：20
• 期：7
• 页码：272-276
• 全文大小：652 K

文摘

Hydrophobic insertion of the acyl chain into the bilayer is necessary but not sufficient for the membrane binding of a myristoylated protein. The myristoylated alanine-rich C kinase substrate (MARCKS), Src, ADP-ribosylation factor and human immunodeficiency virus-1 matrix proteins also contain a cluster of basic residues that bind to acidic phospholipids; the hydrophobic and electrostatic interactions act together to anchor the protein to a membrane. For MARCKS, and perhaps other proteins, phosphorylation of serines within its basic cluster reduces the electrostatic attraction, producing translocation of the protein from the membrane to the cytosol by a simple ‘electrostatic switch’ mechanism. Publisher: Elsevier Science Language of Publication: English Item Identifier: S0968-0004(00)89042-8 Publication Type: Miscellaneous ISSN: 0968-0004 Cited by:

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Footnotes:

1. Note: Nucleotide sequence data reported in this paper are available in the EMBL, GenBank and DDJB databases under the accession number X99763.