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

Gopal, Sandeep LU orcid ; Bober, Adam ; Whiteford, James R ; Multhaupt, Hinke A B ; Yoneda, Atsuko and Couchman, John R (2010) In The Journal of biological chemistry 285(19). p.14247-14258
Abstract

Fibroblasts null for the transmembrane proteoglycan, syndecan-4, have an altered actin cytoskeleton, compared with 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, whereas 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... (More)

Fibroblasts null for the transmembrane proteoglycan, syndecan-4, have an altered actin cytoskeleton, compared with 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, whereas 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.

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author
; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Actins/metabolism, Amino Acid Sequence, Animals, Blotting, Western, COS Cells, Cell Adhesion, Cells, Cultured, Chlorocebus aethiops, Cytoskeleton/metabolism, Embryo, Mammalian/cytology, Fibroblasts/metabolism, Fibronectins/metabolism, Focal Adhesion Protein-Tyrosine Kinases/metabolism, Heparitin Sulfate/physiology, Humans, Mice, Mice, Knockout, Microscopy, Fluorescence, Molecular Sequence Data, Phosphorylation, Proteoglycans/metabolism, Syndecan-4/physiology
in
The Journal of biological chemistry
volume
285
issue
19
pages
14247 - 14258
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • pmid:20154082
  • scopus:77951994425
ISSN
1083-351X
DOI
10.1074/jbc.M109.056945
language
English
LU publication?
no
id
32e4920a-5532-48da-9fde-178e8f6248ad
date added to LUP
2021-10-25 13:22:34
date last changed
2025-10-14 10:13:17
@article{32e4920a-5532-48da-9fde-178e8f6248ad,
  abstract     = {{<p>Fibroblasts null for the transmembrane proteoglycan, syndecan-4, have an altered actin cytoskeleton, compared with 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, whereas 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.</p>}},
  author       = {{Gopal, Sandeep and Bober, Adam and Whiteford, James R and Multhaupt, Hinke A B and Yoneda, Atsuko and Couchman, John R}},
  issn         = {{1083-351X}},
  keywords     = {{Actins/metabolism; Amino Acid Sequence; Animals; Blotting, Western; COS Cells; Cell Adhesion; Cells, Cultured; Chlorocebus aethiops; Cytoskeleton/metabolism; Embryo, Mammalian/cytology; Fibroblasts/metabolism; Fibronectins/metabolism; Focal Adhesion Protein-Tyrosine Kinases/metabolism; Heparitin Sulfate/physiology; Humans; Mice; Mice, Knockout; Microscopy, Fluorescence; Molecular Sequence Data; Phosphorylation; Proteoglycans/metabolism; Syndecan-4/physiology}},
  language     = {{eng}},
  number       = {{19}},
  pages        = {{14247--14258}},
  publisher    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{The Journal of biological chemistry}},
  title        = {{Heparan sulfate chain valency controls syndecan-4 function in cell adhesion}},
  url          = {{http://dx.doi.org/10.1074/jbc.M109.056945}},
  doi          = {{10.1074/jbc.M109.056945}},
  volume       = {{285}},
  year         = {{2010}},
}