Emerin caps the pointed end of actin filaments: Evidence for an actin cortical network at the nuclear inner membrane

被引:171
作者
Holaska, JM [1 ]
Kowalski, AK [1 ]
Wilson, KL [1 ]
机构
[1] Johns Hopkins Univ, Sch Med, Dept Cell Biol, Baltimore, MD 21218 USA
关键词
D O I
10.1371/journal.pbio.0020231
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
X-linked Emery-Dreifuss muscular dystrophy is caused by loss of emerin, a LEM-domain protein of the nuclear inner membrane. To better understand emerin function, we used affinity chromatography to purify emerin-binding proteins from nuclear extracts of HeLa cells. Complexes that included actin, all-spectrin and additional proteins, bound specifically to emerin. Actin polymerization assays in the presence or absence of gelsolin or capping protein showed that emerin binds and stabilizes the pointed end of actin filaments, increasing the actin polymerization rate 4- to 12-fold. We propose that emerin contributes to the formation of an actin-based cortical network at the nuclear inner membrane, conceptually analogous to the actin cortical network at the plasma membrane. Thus, in addition to disrupting transcription factors that bind emerin, loss of emerin may destabilize nuclear envelope architecture by weakening a nuclear actin network.
引用
收藏
页码:1354 / 1362
页数:9
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