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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Heparan sulfate chain valency controls syndecan-4 function in cell adhesion. / Gopal, Sandeep; Bober, Adam; Whiteford, James R; Multhaupt, Hinke A B; Yoneda, Atsuko; Couchman, John R.

In: Journal of Biological Chemistry, Vol. 285, No. 19, 12.02.2010, p. 14247-58.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Gopal, S, Bober, A, Whiteford, JR, Multhaupt, HAB, Yoneda, A & Couchman, JR 2010, 'Heparan sulfate chain valency controls syndecan-4 function in cell adhesion', Journal of Biological Chemistry, vol. 285, no. 19, pp. 14247-58. https://doi.org/10.1074/jbc.M109.056945

APA

Gopal, S., Bober, A., Whiteford, J. R., Multhaupt, H. A. B., Yoneda, A., & Couchman, J. R. (2010). Heparan sulfate chain valency controls syndecan-4 function in cell adhesion. Journal of Biological Chemistry, 285(19), 14247-58. https://doi.org/10.1074/jbc.M109.056945

Vancouver

Gopal S, Bober A, Whiteford JR, Multhaupt HAB, Yoneda A, Couchman JR. Heparan sulfate chain valency controls syndecan-4 function in cell adhesion. Journal of Biological Chemistry. 2010 Feb 12;285(19):14247-58. https://doi.org/10.1074/jbc.M109.056945

Author

Gopal, Sandeep ; Bober, Adam ; Whiteford, James R ; Multhaupt, Hinke A B ; Yoneda, Atsuko ; Couchman, John R. / Heparan sulfate chain valency controls syndecan-4 function in cell adhesion. In: Journal of Biological Chemistry. 2010 ; Vol. 285, No. 19. pp. 14247-58.

Bibtex

@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",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "19",

}

RIS

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 -

ID: 18203554