کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10870701 1074018 2014 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Gap junction regulation by calmodulin
ترجمه فارسی عنوان
مقاربت اتصال مجدد توسط کالمدولین
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
چکیده انگلیسی
Intracellular Ca2+ activated calmodulin (CaM) inhibits gap junction channels in the low nanomolar to high micromolar range of [Ca2+]i. This regulation plays an essential role in numerous cellular processes that include hearing, lens transparency, and synchronized contractions of the heart. Previous studies have indicated that gap junction mediated cell-to-cell communication was inhibited by CaM antagonists. More recent evidence indicates a direct role of CaM in regulating several members of the connexin family. Since the intracellular loop and carboxyl termini of connexins are largely “invisible” in electron microscopy and X-ray crystallographic structures due to disorder in these domains, peptide models encompassing the putative CaM binding sites of several intracellular domains of connexins have been used to identify the Ca2+-dependent CaM binding sites of these proteins. This approach has been used to determine the CaM binding affinities of peptides derived from a number of different connexin-subfamilies.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 588, Issue 8, 17 April 2014, Pages 1430-1438
نویسندگان
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