Heparan sulfate chain valency controls syndecan-4 function in cell adhesion

Sandeep Gopal; Adam Bober; James R Whiteford; Hinke A B Multhaupt; Atsuko Yoneda; John R Couchman

doi:10.1074/jbc.M109.056945

Heparan sulfate chain valency controls syndecan-4 function in cell adhesion

Sandeep Gopal, Adam Bober, James R Whiteford, Hinke A B Multhaupt, Atsuko Yoneda, John R Couchman

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

65 Citationer (Scopus)

Abstract

Udgivelsesdato: 2010-Feb-12

Originalsprog	Engelsk
Tidsskrift	Journal of Biological Chemistry
Vol/bind	285
Udgave nummer	19
Sider (fra-til)	14247-58
Antal sider	12
ISSN	0021-9258
DOI	https://doi.org/10.1074/jbc.M109.056945
Status	Udgivet - 12 feb. 2010

Adgang til dokumentet

10.1074/jbc.M109.056945

Citationsformater

@article{fae97b70215011df8ed1000ea68e967b,

title = "Heparan sulfate chain valency controls syndecan-4 function in cell adhesion",

abstract = "Fibroblasts null for the transmembrane proteoglycan, syndecan-4, have an altered actin cytoskeleton, compared to matching wild-type cells. They do not organize alpha-smooth muscle actin into bundles, but will do so when full length syndecan-4 is re-expressed. This requires the central V region of the core protein cytoplasmic domain, though not interactions with PDZ proteins. A second key requirement is multiple heparan sulfate chains. Mutant syndecan-4 with no chains, or only one chain, failed to restore the wild type phenotype, while those expressing two or three were competent. However, clustering of one-chain syndecan-4 forms with antibodies overcame the block, indicating that valency of interactions with ligands is a key component of syndecan-4 function. Measurements of focal contact/adhesion size and focal adhesion kinase phosphorylation correlated with syndecan-4 status and alpha-smooth muscle actin organization, being reduced where syndecan-4 function was compromised by a lack of multiple heparan sulfate chains.",

author = "Sandeep Gopal and Adam Bober and Whiteford, {James R} and Multhaupt, {Hinke A B} and Atsuko Yoneda and Couchman, {John R}",

year = "2010",

month = feb,

day = "12",

doi = "10.1074/jbc.M109.056945",

language = "English",

volume = "285",

pages = "14247--58",

journal = "Journal of Biological Chemistry",

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publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

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TY - JOUR

T1 - Heparan sulfate chain valency controls syndecan-4 function in cell adhesion

AU - Gopal, Sandeep

AU - Bober, Adam

AU - Whiteford, James R

AU - Multhaupt, Hinke A B

AU - Yoneda, Atsuko

AU - Couchman, John R

PY - 2010/2/12

Y1 - 2010/2/12

N2 - Fibroblasts null for the transmembrane proteoglycan, syndecan-4, have an altered actin cytoskeleton, compared to matching wild-type cells. They do not organize alpha-smooth muscle actin into bundles, but will do so when full length syndecan-4 is re-expressed. This requires the central V region of the core protein cytoplasmic domain, though not interactions with PDZ proteins. A second key requirement is multiple heparan sulfate chains. Mutant syndecan-4 with no chains, or only one chain, failed to restore the wild type phenotype, while those expressing two or three were competent. However, clustering of one-chain syndecan-4 forms with antibodies overcame the block, indicating that valency of interactions with ligands is a key component of syndecan-4 function. Measurements of focal contact/adhesion size and focal adhesion kinase phosphorylation correlated with syndecan-4 status and alpha-smooth muscle actin organization, being reduced where syndecan-4 function was compromised by a lack of multiple heparan sulfate chains.

AB - Fibroblasts null for the transmembrane proteoglycan, syndecan-4, have an altered actin cytoskeleton, compared to matching wild-type cells. They do not organize alpha-smooth muscle actin into bundles, but will do so when full length syndecan-4 is re-expressed. This requires the central V region of the core protein cytoplasmic domain, though not interactions with PDZ proteins. A second key requirement is multiple heparan sulfate chains. Mutant syndecan-4 with no chains, or only one chain, failed to restore the wild type phenotype, while those expressing two or three were competent. However, clustering of one-chain syndecan-4 forms with antibodies overcame the block, indicating that valency of interactions with ligands is a key component of syndecan-4 function. Measurements of focal contact/adhesion size and focal adhesion kinase phosphorylation correlated with syndecan-4 status and alpha-smooth muscle actin organization, being reduced where syndecan-4 function was compromised by a lack of multiple heparan sulfate chains.

U2 - 10.1074/jbc.M109.056945

DO - 10.1074/jbc.M109.056945

M3 - Journal article

C2 - 20154082

VL - 285

SP - 14247

EP - 14258

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 19

ER -