McLaughlin S, Aderem A
Department of Physiology and Biophysics, HSC, SUNY, Stony Brook, NY 11794-8661, USA.
Trends Biochem Sci. 1995 Jul;20(7):272-6. doi: 10.1016/s0968-0004(00)89042-8.
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.
酰基链疏水插入双层膜对于豆蔻酰化蛋白的膜结合是必要的，但并不充分。富含豆蔻酰化丙氨酸的C激酶底物（MARCKS）、Src、ADP核糖基化因子和人类免疫缺陷病毒1型基质蛋白还含有一簇与酸性磷脂结合的碱性残基；疏水相互作用和静电相互作用共同作用将蛋白质锚定在膜上。对于MARCKS以及可能的其他蛋白质，其碱性簇内丝氨酸的磷酸化会降低静电吸引力，通过简单的“静电开关”机制使蛋白质从膜转移到细胞质中。
