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Expression cloning of TGF-β receptors

✍ Scribed by Herbert Y. Lin; Dr. Xiao-Fan Wang

Book ID
102951584
Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
551 KB
Volume
32
Category
Article
ISSN
1040-452X

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✦ Synopsis

Abstract

Using a powerful expression cloning method in COS cells, we have cloned the TGF‐β types II and III receptors. The type III TGF‐β receptor is a membrane‐bound proteoglycan with a core protein of about 110 kDa. Stable expression of the type III receptor in L6 myoblasts leads to an apparent increase in the ability of the type II receptor to bind iodinated TGF‐β1. The cloned type II receptor has a predicted protein core of about 60 kDa with a cysteine‐rich extracellular domain, a single transmembrane domain, and a functional serine/threonine kinase domain that is homologous to the activin receptor and to the C. elegans protein daf‐1. These results implicate serine/threonine phosphorylation as an important mechanism of TGF‐β action. © 1992 Wiley‐Liss, Inc.

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## Abstract The nature and role of cell surface proteins that bind members of the TGF‐β family has been investigated. TGF‐β, activins, and BMPs each bind to receptors of 55 kDa (type I) and 70 kDa (type II). In the TGF‐β system, these receptors are implicated in the mediation of multiple responses.