生物物理
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
in vivo及びin vitroにおける蛋白質のアシル化と機能制御
内海 俊彦
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ジャーナル フリー

1992 年 32 巻 5 号 p. 243-248

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A large number of proteins of diverse origin are being found to undergo covalent modification by the addition of long-chain, saturated fatty acids such as myristate and palmitate. Many of these acylated proteins appear to play critical roles in transmembrane regulatory pathways in cells by modulating the reversible association of these proteins with membrane. Fatty acid moiety of the acylated protein seems to enhance the affinity of the protein to the phospholipid bilayer and the membrane binding is then stabilized by the association with a specific membrane protein, The protein-membrane interaction is also regulated by protein-phosphorylation and/or acylation-deacylation cycle of these acylated proteins.
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© by THE BIOPHYSICAL SOCIETY OF JAPAN
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