کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2052207 1074224 2006 4 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A caldesmon peptide activates smooth muscle via a mechanism similar to ERK-mediated phosphorylation
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
A caldesmon peptide activates smooth muscle via a mechanism similar to ERK-mediated phosphorylation
چکیده انگلیسی

Caldesmon (CaD) is thought to regulate smooth muscle contraction, because it binds actin and inhibits actomyosin interactions. A synthetic actin-binding peptide (GS17C) corresponding to Gly666–Ser682 of chicken gizzard CaD has been shown to induce force development in permeabilized smooth muscle cells. The mechanism of GS17C’s action remains unclear, although a structural effect was postulated. By photo-crosslinking and fluorescence quenching experiments with a gizzard CaD fragment (H32K; Met563-Pro771) and its mutants, we showed that GS17C indeed dissociated the C-terminal region of H32K from actin, in a manner similar to extracellular signal-regulated kinase-mediated phosphorylation, thereby reversing the CaD-imposed inhibition and enabling the actomyosin interaction.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 1, 9 January 2006, Pages 63–66
نویسندگان
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