Syndecan proteoglycan contributions to cytoskeletal organization and contractility

E Okina; T Manon-Jensen; J R Whiteford; J R Couchman

doi:10.1111/j.1600-0838.2009.00941.x

Syndecan proteoglycan contributions to cytoskeletal organization and contractility

E Okina, T Manon-Jensen, J R Whiteford, J R Couchman

Nutritional Immunology

35 Citations (Scopus)

Abstract

Cells exert tension on the extracellular matrix through specific receptors that link to the actin cytoskeleton. The best characterized are the integrins, which, when activated and clustered, can link to the extracellular matrix at specialized adhesion zones, known as focal contacts or focal adhesions. However, other transmembrane receptors can also localize there, including one transmembrane proteoglycan, syndecan-4. This heparan sulfate proteoglycan can also link directly to the cytoskeleton through alpha-actinin, and can signal through protein kinase C. In turn, the pathway leads to RhoA and Rho kinases that control actomyosin contractility. Syndecan-4 may, therefore, be a sensor of tension exerted on the matrix. These processes are described here, their significance being potential roles in wound contraction, tumor-stroma interactions, fibrosis and the regulation of motility.

Original language	English
Journal	Scandinavian Journal of Medicine & Science in Sports Online
ISSN	1600-0838
DOIs	https://doi.org/10.1111/j.1600-0838.2009.00941.x
Publication status	Published - 2009

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title = "Syndecan proteoglycan contributions to cytoskeletal organization and contractility",

abstract = "Cells exert tension on the extracellular matrix through specific receptors that link to the actin cytoskeleton. The best characterized are the integrins, which, when activated and clustered, can link to the extracellular matrix at specialized adhesion zones, known as focal contacts or focal adhesions. However, other transmembrane receptors can also localize there, including one transmembrane proteoglycan, syndecan-4. This heparan sulfate proteoglycan can also link directly to the cytoskeleton through alpha-actinin, and can signal through protein kinase C. In turn, the pathway leads to RhoA and Rho kinases that control actomyosin contractility. Syndecan-4 may, therefore, be a sensor of tension exerted on the matrix. These processes are described here, their significance being potential roles in wound contraction, tumor-stroma interactions, fibrosis and the regulation of motility.",

author = "E Okina and T Manon-Jensen and Whiteford, {J R} and Couchman, {J R}",

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doi = "10.1111/j.1600-0838.2009.00941.x",

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T1 - Syndecan proteoglycan contributions to cytoskeletal organization and contractility

AU - Okina, E

AU - Manon-Jensen, T

AU - Whiteford, J R

AU - Couchman, J R

PY - 2009

Y1 - 2009

N2 - Cells exert tension on the extracellular matrix through specific receptors that link to the actin cytoskeleton. The best characterized are the integrins, which, when activated and clustered, can link to the extracellular matrix at specialized adhesion zones, known as focal contacts or focal adhesions. However, other transmembrane receptors can also localize there, including one transmembrane proteoglycan, syndecan-4. This heparan sulfate proteoglycan can also link directly to the cytoskeleton through alpha-actinin, and can signal through protein kinase C. In turn, the pathway leads to RhoA and Rho kinases that control actomyosin contractility. Syndecan-4 may, therefore, be a sensor of tension exerted on the matrix. These processes are described here, their significance being potential roles in wound contraction, tumor-stroma interactions, fibrosis and the regulation of motility.

AB - Cells exert tension on the extracellular matrix through specific receptors that link to the actin cytoskeleton. The best characterized are the integrins, which, when activated and clustered, can link to the extracellular matrix at specialized adhesion zones, known as focal contacts or focal adhesions. However, other transmembrane receptors can also localize there, including one transmembrane proteoglycan, syndecan-4. This heparan sulfate proteoglycan can also link directly to the cytoskeleton through alpha-actinin, and can signal through protein kinase C. In turn, the pathway leads to RhoA and Rho kinases that control actomyosin contractility. Syndecan-4 may, therefore, be a sensor of tension exerted on the matrix. These processes are described here, their significance being potential roles in wound contraction, tumor-stroma interactions, fibrosis and the regulation of motility.

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DO - 10.1111/j.1600-0838.2009.00941.x

M3 - Journal article

C2 - 19538537

SN - 1600-0838

JO - Scandinavian Journal of Medicine & Science in Sports Online

JF - Scandinavian Journal of Medicine & Science in Sports Online

ER -

Syndecan proteoglycan contributions to cytoskeletal organization and contractility

Abstract

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