Syndecan-4 associates with alpha-actinin.

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

Standard

Syndecan-4 associates with alpha-actinin. / Greene, Daniel K; Tumova, Sarka; Couchman, John R; Woods, Anne.

In: Journal of Biological Chemistry, Vol. 278, No. 9, 2002, p. 7617-23.

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

Harvard

Greene, DK, Tumova, S, Couchman, JR & Woods, A 2002, 'Syndecan-4 associates with alpha-actinin.', Journal of Biological Chemistry, vol. 278, no. 9, pp. 7617-23. https://doi.org/10.1074/jbc.M207123200

APA

Greene, D. K., Tumova, S., Couchman, J. R., & Woods, A. (2002). Syndecan-4 associates with alpha-actinin. Journal of Biological Chemistry, 278(9), 7617-23. https://doi.org/10.1074/jbc.M207123200

Vancouver

Greene DK, Tumova S, Couchman JR, Woods A. Syndecan-4 associates with alpha-actinin. Journal of Biological Chemistry. 2002;278(9):7617-23. https://doi.org/10.1074/jbc.M207123200

Author

Greene, Daniel K ; Tumova, Sarka ; Couchman, John R ; Woods, Anne. / Syndecan-4 associates with alpha-actinin. In: Journal of Biological Chemistry. 2002 ; Vol. 278, No. 9. pp. 7617-23.

Bibtex

@article{b660d6d0596d11dd8d9f000ea68e967b,
title = "Syndecan-4 associates with alpha-actinin.",
abstract = "Cell adhesion to the extracellular matrix influences many cellular functions. The integrin family of matrix receptors plays major roles in the formation of adhesions, but other proteins modulate integrin signaling. Syndecan-4, a transmembrane proteoglycan, cooperatively signals with integrins during the formation of focal adhesions. To date, a direct link between syndecan-4 and the cytoskeleton has remained elusive. We now demonstrate by Triton X-100 extraction immunoprecipitation and in vitro binding assays that the focal adhesion component alpha-actinin interacts with syndecan-4 in a beta-integrin-independent manner.",
author = "Greene, {Daniel K} and Sarka Tumova and Couchman, {John R} and Anne Woods",
note = "Keywords: Actinin; Amino Acid Sequence; Animals; Cell Adhesion; Cells, Cultured; Cytoskeleton; Detergents; Humans; Membrane Glycoproteins; Microscopy, Fluorescence; Molecular Sequence Data; Octoxynol; Precipitin Tests; Protein Binding; Protein Kinase C; Protein Kinase C-alpha; Protein Structure, Tertiary; Proteoglycans; Rats; Sequence Homology, Amino Acid; Syndecan-4",
year = "2002",
doi = "10.1074/jbc.M207123200",
language = "English",
volume = "278",
pages = "7617--23",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "9",

}

RIS

TY - JOUR

T1 - Syndecan-4 associates with alpha-actinin.

AU - Greene, Daniel K

AU - Tumova, Sarka

AU - Couchman, John R

AU - Woods, Anne

N1 - Keywords: Actinin; Amino Acid Sequence; Animals; Cell Adhesion; Cells, Cultured; Cytoskeleton; Detergents; Humans; Membrane Glycoproteins; Microscopy, Fluorescence; Molecular Sequence Data; Octoxynol; Precipitin Tests; Protein Binding; Protein Kinase C; Protein Kinase C-alpha; Protein Structure, Tertiary; Proteoglycans; Rats; Sequence Homology, Amino Acid; Syndecan-4

PY - 2002

Y1 - 2002

N2 - Cell adhesion to the extracellular matrix influences many cellular functions. The integrin family of matrix receptors plays major roles in the formation of adhesions, but other proteins modulate integrin signaling. Syndecan-4, a transmembrane proteoglycan, cooperatively signals with integrins during the formation of focal adhesions. To date, a direct link between syndecan-4 and the cytoskeleton has remained elusive. We now demonstrate by Triton X-100 extraction immunoprecipitation and in vitro binding assays that the focal adhesion component alpha-actinin interacts with syndecan-4 in a beta-integrin-independent manner.

AB - Cell adhesion to the extracellular matrix influences many cellular functions. The integrin family of matrix receptors plays major roles in the formation of adhesions, but other proteins modulate integrin signaling. Syndecan-4, a transmembrane proteoglycan, cooperatively signals with integrins during the formation of focal adhesions. To date, a direct link between syndecan-4 and the cytoskeleton has remained elusive. We now demonstrate by Triton X-100 extraction immunoprecipitation and in vitro binding assays that the focal adhesion component alpha-actinin interacts with syndecan-4 in a beta-integrin-independent manner.

U2 - 10.1074/jbc.M207123200

DO - 10.1074/jbc.M207123200

M3 - Journal article

C2 - 12493766

VL - 278

SP - 7617

EP - 7623

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 9

ER -

ID: 5162703