کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2188669 1096181 2007 13 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Arrestin Mobilizes Signaling Proteins to the Cytoskeleton and Redirects their Activity
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
Arrestin Mobilizes Signaling Proteins to the Cytoskeleton and Redirects their Activity
چکیده انگلیسی

Arrestins regulate the activity and subcellular localization of G protein-coupled receptors and other signaling molecules. Here, we demonstrate that arrestins bind microtubules (MTs) in vitro and in vivo. The MT-binding site on arrestins overlaps significantly with the receptor-binding site, but the conformations of MT-bound and receptor-bound arrestin are different. Arrestins recruit ERK1/2 and the E3 ubiquitin ligase Mdm2 to MTs in cells, similar to the arrestin-dependent mobilization of these proteins to the receptor. Arrestin-mediated sequestration of ERK to MTs reduces the level of ERK activation. In contrast, recruitment of Mdm2 to MTs by arrestin channels Mdm2 activity toward cytoskeleton-associated proteins, increasing their ubiquitination dramatically. The mobilization of signaling molecules to MTs is a novel biological function of arrestin proteins.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 368, Issue 2, 27 April 2007, Pages 375–387
نویسندگان
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