The integrin-actin connection, an eternal love affair.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

The integrin-actin connection, an eternal love affair. / Brakebusch, Cord; Fässler, Reinhard.

I: EMBO Journal, Bind 22, Nr. 10, 2003, s. 2324-33.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Brakebusch, C & Fässler, R 2003, 'The integrin-actin connection, an eternal love affair.', EMBO Journal, bind 22, nr. 10, s. 2324-33. https://doi.org/10.1093/emboj/cdg245

APA

Brakebusch, C., & Fässler, R. (2003). The integrin-actin connection, an eternal love affair. EMBO Journal, 22(10), 2324-33. https://doi.org/10.1093/emboj/cdg245

Vancouver

Brakebusch C, Fässler R. The integrin-actin connection, an eternal love affair. EMBO Journal. 2003;22(10):2324-33. https://doi.org/10.1093/emboj/cdg245

Author

Brakebusch, Cord ; Fässler, Reinhard. / The integrin-actin connection, an eternal love affair. I: EMBO Journal. 2003 ; Bind 22, Nr. 10. s. 2324-33.

Bibtex

@article{af05d7b0589511dd8d9f000ea68e967b,
title = "The integrin-actin connection, an eternal love affair.",
abstract = "Integrin receptors connect the extracellular matrix to the actin cytoskeleton. This interaction can be viewed as a cyclical liaison, which develops again and again at new adhesion sites only to cease at sites of de-adhesion. Recent work has demonstrated that multidomain proteins play crucial roles in the integrin-actin connection by providing a high degree of regulation adjusted to the needs of the cell. In this review we present several examples of this paradigm and with special emphasis on the ILK-PINCH-parvin complex, which amply demonstrates how structural and signalling functions are linked together.",
author = "Cord Brakebusch and Reinhard F{\"a}ssler",
note = "Keywords: Actinin; Actins; Animals; Carrier Proteins; Cell Adhesion; Cytoskeleton; DNA-Binding Proteins; Extracellular Matrix; Focal Adhesion Protein-Tyrosine Kinases; Integrins; Intracellular Signaling Peptides and Proteins; Membrane Proteins; Microfilament Proteins; Protein-Serine-Threonine Kinases; Protein-Tyrosine Kinases; Signal Transduction",
year = "2003",
doi = "10.1093/emboj/cdg245",
language = "English",
volume = "22",
pages = "2324--33",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "10",

}

RIS

TY - JOUR

T1 - The integrin-actin connection, an eternal love affair.

AU - Brakebusch, Cord

AU - Fässler, Reinhard

N1 - Keywords: Actinin; Actins; Animals; Carrier Proteins; Cell Adhesion; Cytoskeleton; DNA-Binding Proteins; Extracellular Matrix; Focal Adhesion Protein-Tyrosine Kinases; Integrins; Intracellular Signaling Peptides and Proteins; Membrane Proteins; Microfilament Proteins; Protein-Serine-Threonine Kinases; Protein-Tyrosine Kinases; Signal Transduction

PY - 2003

Y1 - 2003

N2 - Integrin receptors connect the extracellular matrix to the actin cytoskeleton. This interaction can be viewed as a cyclical liaison, which develops again and again at new adhesion sites only to cease at sites of de-adhesion. Recent work has demonstrated that multidomain proteins play crucial roles in the integrin-actin connection by providing a high degree of regulation adjusted to the needs of the cell. In this review we present several examples of this paradigm and with special emphasis on the ILK-PINCH-parvin complex, which amply demonstrates how structural and signalling functions are linked together.

AB - Integrin receptors connect the extracellular matrix to the actin cytoskeleton. This interaction can be viewed as a cyclical liaison, which develops again and again at new adhesion sites only to cease at sites of de-adhesion. Recent work has demonstrated that multidomain proteins play crucial roles in the integrin-actin connection by providing a high degree of regulation adjusted to the needs of the cell. In this review we present several examples of this paradigm and with special emphasis on the ILK-PINCH-parvin complex, which amply demonstrates how structural and signalling functions are linked together.

U2 - 10.1093/emboj/cdg245

DO - 10.1093/emboj/cdg245

M3 - Journal article

C2 - 12743027

VL - 22

SP - 2324

EP - 2333

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 10

ER -

ID: 5141360