کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2166409 1091853 2009 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The self-association of two N-terminal interaction domains plays an important role in the tetramerization of TRPC4
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
The self-association of two N-terminal interaction domains plays an important role in the tetramerization of TRPC4
چکیده انگلیسی

Transient receptor potential canonical (TRPC) channels function as cation channels. In a previous study, we identified the molecular determinants involved in promoting TRPC subunit assembly. In the present study, we used size-exclusion chromatography assays to show that the N-terminus of TRPC4 can self-associate and form a tetramer in cellulo. We further showed that the N-terminus of TRPC4 self-associates via the ankyrin repeat domain and the region downstream from the coiled-coil domain. GST pull-down, yeast two-hybrid, and circular dichroism approaches demonstrated that both domains can self-associate. These findings indicated that the self-association of two distinct domains in the N-terminus of TRPC4 is involved in the assembly of the tetrameric channel.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cell Calcium - Volume 45, Issue 3, March 2009, Pages 251–259
نویسندگان
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