کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9015879 | 1127582 | 2005 | 16 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Macromolecular complexes of cystic fibrosis transmembrane conductance regulator and its interacting partners
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کلمات کلیدی
ABCPDZ proteinPDZK1cGKIIROMKNHERFezrin-radixin-moesinAKAPβ2ARPDZAP-2EBP50SNARECFTRAFMMSDERMAMPKENaC - ENACAmino - آمینوFluorescence resonance energy transfer - انتقال انرژی رزونانس Fluorescencebioluminescence resonance energy transfer - انتقال انرژی رزونانس بیولومینسانسFRET - انتقال انرژی رزونانسی فورسترBRET - برتmembrane-spanning domain - دامنه غشاییcystic fibrosis transmembrane conductance regulator - رگولاتور رسانایی فرابنفش فیبروز کیستیکendoplasmic reticulum - شبکه آندوپلاسمی transmembrane - فرابنفشCystic fibrosis - فیبروز کیستیکRegulatory - مقرراتatomic force microscopy - میکروسکوپ نیروی اتمیA-kinase anchoring protein - پروتئین anchoring A-kinaseMacromolecular complex - پیچیدگی مولکولیCarboxyl - کاربوکسیلcal - کالEpithelial Na+ channel - کانال نیکل Epithelial +ATP-binding cassette - کیت اتصال به ATPAMP-activated kinase - کیناز فعال AMPsoluble NSF attachment protein receptor - گیرنده پروتئینی پروتئین دلبستگی NSF محلول است
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
داروشناسی
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چکیده انگلیسی
The cystic fibrosis transmembrane conductance regulator (CFTR) is the product of the gene mutated in patients with cystic fibrosis (CF). CFTR is a cAMP-regulated chloride channel localized primarily at the apical or luminal surfaces of epithelial cells lining the airway, gut, exocrine glands, etc., where it is responsible for transepithelial salt and water transport. CFTR chloride channel belongs to the superfamily of the ATP-binding cassette (ABC) transporters, which bind ATP and use the energy to drive the transport of a wide variety of substrates across extra- and intracellular membranes. A growing number of proteins have been reported to interact directly or indirectly with CFTR chloride channel, suggesting that CFTR might regulate the activities of other ion channels, receptors, or transporters, in addition to its role as a chloride conductor. The molecular assembly of CFTR with these interacting proteins is of great interest and importance because several human diseases are attributed to altered regulation of CFTR, among which cystic fibrosis is the most serious one. Most interactions primarily occur between the opposing terminal tails (N- or C-) of CFTR and its binding partners, either directly or mediated through various PDZ domain-containing proteins. These dynamic interactions impact the channel function as well as the localization and processing of CFTR protein within cells. This review focuses on the recent developments in defining the assembly of CFTR-containing complexes in the plasma membrane and its interacting proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Pharmacology & Therapeutics - Volume 108, Issue 2, November 2005, Pages 208-223
Journal: Pharmacology & Therapeutics - Volume 108, Issue 2, November 2005, Pages 208-223
نویسندگان
Chunying Li, Anjaparavanda P. Naren,