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  The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!

Wickström, S. A., Lange, A., Montanez, E., & Fassler, R. (2010). The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase! EMBO J, 29(2), 281-91. doi:10.1038/emboj.2009.376.

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Genre: Zeitschriftenartikel

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https://www.ncbi.nlm.nih.gov/pubmed/20033063 (beliebiger Volltext)
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 Urheber:
Wickström, S. A.1, Autor           
Lange, A., Autor
Montanez, E., Autor
Fassler, R., Autor
Affiliations:
1Wickström – Skin Homeostasis and Ageing, Max Planck Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942298              

Inhalt

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Schlagwörter: Amino Acid Sequence Animals DNA-Binding Proteins/genetics/*metabolism Humans Microfilament Proteins/genetics/*metabolism Molecular Sequence Data Morphogenesis Protein-Serine-Threonine Kinases/genetics/*metabolism Sequence Alignment
 Zusammenfassung: Dynamic interactions of cells with their environment regulate multiple aspects of tissue morphogenesis and function. Integrins are the major class of cell surface receptors that recognize and bind extracellular matrix proteins, resulting in the engagement and organization of the cytoskeleton as well as activation of signalling pathways to regulate cell behaviour and morphogenetic processes. The ternary complex of integrin-linked kinase (ILK), PINCH, and parvin (IPP complex), which was identified more than a decade ago, interacts with the cytoplasmic tail of beta integrins and couples them to the actin cytoskeleton. In addition, ILK has been shown to act as a serine/threonine kinase and to directly activate several signalling pathways downstream of integrins. However, the kinase activity of ILK and the precise functions of the IPP complex have remained elusive and controversial. This review focuses on the recent advances made towards understanding the specialized roles this complex and its individual components have acquired during evolution.

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 Datum: 2010-01-202010
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: Anderer: 20033063
DOI: 10.1038/emboj.2009.376
ISSN: 1460-2075 (Electronic)0261-4189 (Linking)
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Titel: EMBO J
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 29 (2) Artikelnummer: - Start- / Endseite: 281 - 91 Identifikator: -