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Transmembrane Signaling Proteoglycans

Couchman, John R.·2010·Annual Review of Cell and Developmental Biology

Abstract

Virtually all metazoan cells contain at least one and usually several types of transmembrane proteoglycans. These are varied in protein structure and type of polysaccharide, but the total number of vertebrate genes encoding transmembrane proteoglycan core proteins is less than 10. Some core proteins, including those of the syndecans, always possess covalently coupled glycosaminoglycans; others do not. Syndecan has a long evolutionary history, as it is present in invertebrates, but many other transmembrane proteoglycans are vertebrate inventions. The variety of proteins and their glycosaminoglycan chains is matched by diverse functions. However, all assume roles as coreceptors, often working alongside high-affinity growth factor receptors or adhesion receptors such as integrins. Other common themes are an ability to signal through their cytoplasmic domains, often to the actin cytoskeleton, and linkage to PDZ protein networks. Many transmembrane proteoglycans associate on the cell surface with metzincin proteases and can be shed by them. Work with model systems in vivo and in vitro reveals roles in growth, adhesion, migration, and metabolism. Furthermore, a wide range of phenotypes for the core proteins has been obtained in mouse knockout experiments. Here some of the latest developments in the field are examined in hopes of stimulating further interest in this fascinating group of molecules.

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Metadata

Authors
Couchman, J. R.
Venue
Annual Review of Cell and Developmental Biology
Published
2010-11-10
Volume
26
Issue
1
Pages
89-114
ISSN
  • 1081-0706 (ISSN-L)
  • 1530-8995
OpenAlex
W2103048323
Cited by
403
References
7
FWCI
2.02
Type
journal article
Language
en
Open access
closed

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