Integrin-linked kinase is an adaptor with essential functions during mouse development

Anika Lange, Sara A. Wickström, Madis Jakobson, Roy Zent, Kirsi Sainio and Reinhard Fässler ()
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Anika Lange: Max Planck Institute of Biochemistry
Sara A. Wickström: Max Planck Institute of Biochemistry
Madis Jakobson: Institute of Biomedicine, Medical Biochemistry and Developmental Biology, University of Helsinki
Roy Zent: Vanderbilt Medical Center and Veterans Affairs Hospital, Nashville, Tennessee 37232, USA
Kirsi Sainio: Institute of Biomedicine, Medical Biochemistry and Developmental Biology, University of Helsinki
Reinhard Fässler: Max Planck Institute of Biochemistry

Nature, 2009, vol. 461, issue 7266, 1002-1006

Abstract: Support role for ILK Integrin-linked kinase (ILK) binds to the cytoplasmic domains of β-integrins and regulates actin dynamics by recruiting actin-binding regulatory proteins such as α- and β-parvin. Previous studies have suggested that ILK has serine/threonine kinase activity and can phosphorylate a number of signalling proteins. Here Fässler and colleagues make transgenic mice carrying point mutations in the proposed autophosphorylation site of the putative kinase domain (KD) and in the pleckstrin homology (PH) domain of ILK. In these mice, developmental processes, tissue function, phosphorylation of key substrates and actin-dependent processes downstream of integrin signalling are normal. However, mice carrying a point mutation that inhibits binding to α-parvin do not survive owing to kidney defects. These results suggest that ILK functions as a scaffolding protein.

Date: 2009
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DOI: 10.1038/nature08468

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