Transduction of Receptor Signals by ß - Arrestins

نویسندگان

  • Robert J. Lefkowitz
  • Sudha K. Shenoy
چکیده

www.sciencemag.org (this information is current as of January 12, 2009 ): The following resources related to this article are available online at http://www.sciencemag.org/cgi/content/full/308/5721/512 version of this article at: including high-resolution figures, can be found in the online Updated information and services, http://www.sciencemag.org/cgi/content/full/308/5721/512/DC1 can be found at: Supporting Online Material found at: can be related to this article A list of selected additional articles on the Science Web sites http://www.sciencemag.org/cgi/content/full/308/5721/512#otherarticles , 44 of which can be accessed for free: cites 61 articles This article http://www.sciencemag.org/cgi/content/full/308/5721/512#otherarticles 97 articles hosted by HighWire Press; see: cited by This article has been http://www.sciencemag.org/cgi/collection/cell_biol Cell Biology : subject collections This article appears in the following http://www.sciencemag.org/about/permissions.dtl in whole or in part can be found at: this article permission to reproduce of this article or about obtaining reprints Information about obtaining

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Cardiorenal actions of TRV120027, a novel ß-arrestin-biased ligand at the angiotensin II type I receptor, in healthy and heart failure canines: a novel therapeutic strategy for acute heart failure.

BACKGROUND The angiotensin II type 1 receptor (AT1R) plays a key role in regulating cardiorenal function. Classic "unbiased" AT1R antagonists block receptor coupling to both G(αq) and ß-arrestin-mediated signals, which desensitize G-protein signaling as well as transduce G-protein-independent signals. TRV120027 is a novel ß-arrestin-biased AT1R ligand, which engages ß-arrestins while blocking G...

متن کامل

The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals.

beta-Arrestins are versatile adapter proteins that form complexes with most G-protein-coupled receptors (GPCRs) following agonist binding and phosphorylation of receptors by G-protein-coupled receptor kinases (GRKs). They play a central role in the interrelated processes of homologous desensitization and GPCR sequestration, which lead to the termination of G protein activation. beta-arrestin bi...

متن کامل

Distinct phosphorylation sites on the ghrelin receptor, GHSR1a, establish a code that determines the functions of ß-arrestins

The growth hormone secretagogue receptor, GHSR1a, mediates the biological activities of ghrelin, which includes the secretion of growth hormone, as well as the stimulation of appetite, food intake and maintenance of energy homeostasis. Mapping phosphorylation sites on GHSR1a and knowledge of how these sites control specific functional consequences unlocks new strategies for the development of t...

متن کامل

Arrestins as signaling molecules involved in apoptotic pathways: a real eye opener.

Recent data suggest that internalized receptor and arrestin complexes are actively involved in signal transduction. Miller and Lefkowitz discuss evidence from the Drosophila visual system that suggests that intracellular rhodopsin and arrestin2 complexes induce apoptosis. Experiments with activated mammalian G protein-coupled receptor and arrestin complexes point to a mechanism by which prolife...

متن کامل

GRKs and beta-arrestins: roles in receptor silencing, trafficking and signaling.

Stimulation of cell-surface seven-transmembrane receptors (7TMRs) elicits biological responses to a wide range of extracellular signals, including many hormones. Classically, heterotrimeric GTP-binding proteins (G proteins) are recruited to the activated conformation of 7TMRs. Only two other families of protein have this remarkable characteristic: G-protein-coupled receptor kinases and beta-arr...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2009