کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2187939 1096147 2008 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Coronin-1A Stabilizes F-Actin by Bridging Adjacent Actin Protomers and Stapling Opposite Strands of the Actin Filament
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
Coronin-1A Stabilizes F-Actin by Bridging Adjacent Actin Protomers and Stapling Opposite Strands of the Actin Filament
چکیده انگلیسی

Coronins are F-actin-binding proteins that are involved, in concert with Arp2/3, Aip1, and ADF/cofilin, in rearrangements of the actin cytoskeleton. An understanding of coronin function has been hampered by the absence of any structural data on its interaction with actin. Using electron microscopy and three-dimensional reconstruction, we show that coronin-1A binds to three protomers in F-actin simultaneously: it bridges subdomain 1 and subdomain 2 of two adjacent actin subunits along the same long-pitch strand, and it staples subdomain 1 and subdomain 4 of two actin protomers on different strands. Such a mode of binding explains how coronin can stabilize actin filaments in vitro. In addition, we show which residues of F-actin may participate in the interaction with coronin-1A. Human nebulin and Xin, as well as Salmonella invasion protein A, use a similar mechanism to stabilize actin filaments. We suggest that the stapling of subdomain 1 and subdomain 4 of two actin protomers on different strands is a common mechanism for F-actin stabilization utilized by many actin-binding proteins that have no homology.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 376, Issue 3, 22 February 2008, Pages 607–613
نویسندگان
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