کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1997049 1065536 2010 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
K11-Linked Polyubiquitination in Cell Cycle Control Revealed by a K11 Linkage-Specific Antibody
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
K11-Linked Polyubiquitination in Cell Cycle Control Revealed by a K11 Linkage-Specific Antibody
چکیده انگلیسی

SummaryPolyubiquitination is a posttranslational modification where ubiquitin chains containing isopeptide bonds linking one of seven ubiquitin lysines with the C terminus of an adjoining ubiquitin are covalently attached to proteins. While functions of K48- and K63-linked polyubiquitin are understood, the role(s) of noncanonical K11-linked chains is less clear. A crystal structure of K11-linked diubiquitin demonstrates a distinct conformation from K48- or K63-linked diubiquitin. We engineered a K11 linkage-specific antibody and use it to demonstrate that K11 chains are highly upregulated in mitotic human cells precisely when substrates of the ubiquitin ligase anaphase-promoting complex (APC/C) are degraded. These chains increased with proteasomal inhibition, suggesting they act as degradation signals in vivo. Inhibition of the APC/C strongly impeded the formation of K11-linked chains, suggesting that a single ubiquitin ligase is the major source of mitotic K11-linked chains. Our results underscore the importance of K11-linked ubiquitin chains as critical regulators of mitotic protein degradation.


► K11-linked diubiquitin adopts a conformation distinct from other diubiquitins
► A K11-linked polyubiquitin-specific antibody was engineered
► UbcH10/Ube2S and APC/C are the major source of mitotic K11-linked chains in vivo
► K11-linked chains act as proteasomal degradation signals in vivo

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 39, Issue 3, 13 August 2010, Pages 477–484
نویسندگان
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