cAMP-dependent phosphorylation of neurofilament proteins NF-L and NF-M inhibits their coassembly into filaments in vitro

被引:16
|
作者
Streifel, TD [1 ]
Avalos, RT [1 ]
Cohlberg, JA [1 ]
机构
[1] CALIF STATE UNIV LONG BEACH,DEPT CHEM & BIOCHEM,LONG BEACH,CA 90840
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
D O I
10.1006/bbrc.1996.0797
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The effects of cAMP-dependent phosphorylation of neurofilament proteins NF-L and NF-M on the coassembly of the two proteins into filaments in vitro was examined. Sedimentation velocity experiments revealed that phosphorylated NF-M sedimented more slowly and resisted salt-induced aggregation. Filaments reconstituted from various mixtures of proteins were pelleted and examined by gel electrophoresis and electron microscopy. Phosphorylation of either protein inhibited the formation of heteropolymer filaments containing NF-L and NF-M. However, phosphorylated proteins were fully competent in forming heterooligomeric assembly intermediates; therefore, phosphorylation blocks a later stage of filament assembly. (C) 1996 Academic Press, Inc.
引用
收藏
页码:646 / 651
页数:6
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