کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1963836 | 1058510 | 2011 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Contribution of a tyrosine-based motif to cellular trafficking of wild-type and truncated NPY Y1 receptors
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کلمات کلیدی
PBSConstitutive internalizationLICGi/oGPCReGFPNPYHEKBSA - BSAG protein-coupled receptors - G گیرنده های پروتئینی همراهbovine serum albumin - آلبومین سرم گاوRecycling - بازیافتInternalization - داخلی سازیPhosphate buffered saline - فسفات بافر شورenhanced green fluorescent protein - پروتئین فلورسنت سبز افزایش یافته استSignal peptide - پپتید سیگنالLigation independent cloning - کلونینگ مستقل انبارداریhuman embryonic kidney - کلیه جنین انسانY1 receptor - گیرنده Y1G protein-coupled receptor - گیرندههای جفتشونده با پروتئین جیNeuropeptide Y - یوروپروتئین Y
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The human NPY Y1 receptor undergoes fast agonist-induced internalization via clathrin-coated pits then recycles back to the cell membrane. In an attempt to identify the molecular determinants involved in this process, we studied several C-terminal truncation mutants tagged with EFGP. In the absence of agonist, Y1 receptors lacking the last 32 C-terminal amino acids (Y1Î32) are constitutively internalized, unlike full-length Y1 receptors. At steady state, internalized Y1Î32 receptors co-localize with transferrin, a marker of early and recycling endosomes. Inhibition of constitutive internalization of Y1Î32 receptors by hypertonic sucrose or by co-expression of Rab5aS34N, a dominant negative form of the small GTPase Rab5a or depletion of all three isoforms of Rab5 indicates the involvement of clathrin-coated pits. In contrast, a truncated receptor lacking the last 42 C-terminal amino acids (Y1Î42) does not constitutively internalize, consistent with the possibility that there is a molecular determinant responsible for constitutive internalization located in the last 10 amino acids of Y1Î32 receptors. We show that the agonist-independent internalization of Y1Î32 receptors involves a tyrosine-based motif YXXΦ. The potential role of this motif in the behaviour of full-length Y1 receptors has also been explored. Our results indicate that a C-terminal tyrosine-based motif is critical for the constitutive internalization of truncated Y1Î32 receptors. We suggest that this motif is masked in full-length Y1 receptors which do not constitutively internalize in the absence of agonist.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 23, Issue 1, January 2011, Pages 228-238
Journal: Cellular Signalling - Volume 23, Issue 1, January 2011, Pages 228-238
نویسندگان
Sandra Lecat, Moussa Ouédraogo, Thomas Cherrier, Fanny Noulet, Philippe Rondé, Nicole Glasser, Jean-Luc Galzi, Yves Mely, Kenneth Takeda, Bernard Bucher,