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Transmembrane Signaling Proteoglycans

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Transmembrane Signaling Proteoglycans. / Couchman, John R.

I: Annual Review of Cell and Developmental Biology, Bind 26, 10.11.2010, s. 89-114.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Couchman, JR 2010, 'Transmembrane Signaling Proteoglycans', Annual Review of Cell and Developmental Biology, bind 26, s. 89-114. https://doi.org/10.1146/annurev-cellbio-100109-104126

APA

Couchman, J. R. (2010). Transmembrane Signaling Proteoglycans. Annual Review of Cell and Developmental Biology, 26, 89-114. https://doi.org/10.1146/annurev-cellbio-100109-104126

Vancouver

Couchman JR. Transmembrane Signaling Proteoglycans. Annual Review of Cell and Developmental Biology. 2010 nov 10;26:89-114. https://doi.org/10.1146/annurev-cellbio-100109-104126

Author

Couchman, John R. / Transmembrane Signaling Proteoglycans. I: Annual Review of Cell and Developmental Biology. 2010 ; Bind 26. s. 89-114.

Bibtex

@article{6ae01060b44011df825b000ea68e967b,
title = "Transmembrane Signaling Proteoglycans",
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 reveal 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. Expected final online publication date for the Annual Review of Cell and Developmental Biology Volume 26 is October 06, 2010. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.",
author = "Couchman, {John R}",
year = "2010",
month = "11",
day = "10",
doi = "10.1146/annurev-cellbio-100109-104126",
language = "English",
volume = "26",
pages = "89--114",
journal = "Annual Review of Cell and Developmental Biology",
issn = "1081-0706",
publisher = "Annual Reviews",

}

RIS

TY - JOUR

T1 - Transmembrane Signaling Proteoglycans

AU - Couchman, John R

PY - 2010/11/10

Y1 - 2010/11/10

N2 - 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 reveal 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. Expected final online publication date for the Annual Review of Cell and Developmental Biology Volume 26 is October 06, 2010. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.

AB - 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 reveal 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. Expected final online publication date for the Annual Review of Cell and Developmental Biology Volume 26 is October 06, 2010. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.

U2 - 10.1146/annurev-cellbio-100109-104126

DO - 10.1146/annurev-cellbio-100109-104126

M3 - Journal article

C2 - 20565253

VL - 26

SP - 89

EP - 114

JO - Annual Review of Cell and Developmental Biology

JF - Annual Review of Cell and Developmental Biology

SN - 1081-0706

ER -

ID: 21664956