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Table of Contents
Vol. 24, No. 2-3, 1998
Issue release date: March – June
Section title: Paper
Miner Electrolyte Metab 1998;24:120–130
(DOI:10.1159/000057359)

TGF-β Receptors and Signalling Mechanisms

Wrana J.L.
Program in Developmental Biology and Division of Gastroenterology, The Hospital for Sick Children and Department of Medical Genetics and Microbiology, University of Toronto, Ont., Canada

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Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: February 23, 1998
Issue release date: March – June

Number of Print Pages: 11
Number of Figures: 2
Number of Tables: 0

ISSN: 0378-0392 (Print)
eISSN: 1423-016X (Online)

For additional information: http://www.karger.com/MEM

Abstract

Transforming growth factor-β (TGF-β) is the founding member of a large superfamily of related growth and differentiation factors that include bone morphogenetic proteins and activins. TGF-β signals through two related transmembrane ser/thr kinase receptors, the type I and type II receptors. Signalling is initiated when the ligand binds to the type II receptor which is followed by recruitment of the type I receptor into a heteromeric complex. Within the complex the type II receptor transphosphorylates and activates the type I receptor kinase which targets downstream signalling components of the pathway. Proteins related to the Drosophila gene Mothers against dpp (MAD) are critical downstream substrates of the type I kinase. The vertebrate members of the MAD-related family, termed Smad 2 and Smad3, interact specifically with the TGF-β type I receptor and are phosphorylated on the last two serines of a conserved C-terminal SSXS motif. This phosphorylation induces association between these receptor-regulated Smads and Smad4 followed by translocation of the heteromeric complex to the nucleus. In the nucleus, heteromeric complexes of Smads can interact with DNA and with specific DNA binding transcription factors to elicit gene responses to TGF-β. Thus TGF-β signalling involves a direct pathway from the cell surface receptors to the nucleus. Recently, a novel mechanism to negatively regulate TGF-β signalling was described that involves another class of MADR proteins. These anti-MADR proteins potently inhibit TGF-β signalling by functioning as direct antagonists of the TGF-β receptor type I kinase domain.


Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: February 23, 1998
Issue release date: March – June

Number of Print Pages: 11
Number of Figures: 2
Number of Tables: 0

ISSN: 0378-0392 (Print)
eISSN: 1423-016X (Online)

For additional information: http://www.karger.com/MEM


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