کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10803140 | 1055795 | 2005 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Identification and characterization of a novel tight junction-associated family of proteins that interacts with a WW domain of MAGI-1
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کلمات کلیدی
PTBGUKMAGI-1PSD-95/DLG/ZO-1LCCPAMOTL1SH3AIPMDCKDRPLAGSTHEK293PDZmembrane-associated guanylate kinase - guanylate kinase مرتبط با غشاءMAGUK - آنهاangiomotin-like 1 - آنژیوموتین مانند 1Tight junction - اتصال تنگphosphotyrosine binding - اتصال فسفاتیروسینYAP - ایجادWW domain - دامنه WWJAM - مرباjunctional adhesion molecule - مولکول چسبندگی مجاورSrc homology 3 - همبستگی Src 3yes-associated protein - پروتئین مرتبط با بلهhuman embryonic kidney 293 - کلیه جنینی انسان 293Madin–Darby Canine Kidney - کلیه کلیوی کلیوی Madin-DarbyCoiled-coil - کویل کویلglutathione-S-transferase - گلوتاتیون S-ترانسفرازGuanylate kinase - گینیلات کیناز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Identification and characterization of a novel tight junction-associated family of proteins that interacts with a WW domain of MAGI-1 Identification and characterization of a novel tight junction-associated family of proteins that interacts with a WW domain of MAGI-1](/preview/png/10803140.png)
چکیده انگلیسی
The membrane-associated guanylate kinase protein, MAGI-1, has been shown to be a component of epithelial tight junctions in both Madin-Darby canine kidney cells and in intestinal epithelium. Because we have previously observed MAGI-1 expression in glomerular visceral epithelial cells (podocytes) of the kidney, we screened a glomerular cDNA library to identify the potential binding partners of MAGI-1 and isolated a partial cDNA encoding a novel protein. The partial cDNA exhibited a high degree of identity to an uncharacterized human cDNA clone, KIAA0989, which encodes a protein of 780 amino acids and contains a predicted coiled-coil domain in the middle of the protein. In vitro binding assays using the partial cDNA as a GST fusion protein confirm the binding to full-length MAGI-1 expressed in HEK293 cells, as well as endogenous MAGI-1, and also identified the first WW domain of MAGI-1 as the domain responsible for binding to this novel protein. Although a conventional PPxY binding motif for WW domains was not present in the partial cDNA clone, a variant WW binding motif was identified, LPxY, and found to be necessary for interacting with MAGI-1. When expressed in Madin-Darby canine kidney cells, the full-length novel protein was found to colocalize with MAGI-1 at the tight junction of these cells and the coiled-coil domain was found to be necessary for this localization. Because of its interaction with MAGI-1 and its localization to cell-cell junctions, this novel protein has been given the name MAGI-1-associated coiled-coil tight junction protein (MASCOT).
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1745, Issue 1, 15 August 2005, Pages 131-144
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1745, Issue 1, 15 August 2005, Pages 131-144
نویسندگان
Kevin M. Patrie,