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¹ Department of Cancer Genetics, British Columbia Cancer Research Centre of the British Columbia Cancer Agency, Vancouver, BC, Canada V5Z 1L3
² Department of Biochemistry and Molecular Biology, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada V6E 4A2

Correspondence to Shoukat Dedhar: sdedhar{at}interchange.ubc.ca

Integrin-linked kinase (ILK) is a serine-threonine kinase and scaffold protein with well defined roles in focal adhesions in integrin-mediated cell adhesion, spreading, migration, and signaling. Using mass spectrometry–based proteomic approaches, we identify centrosomal and mitotic spindle proteins as interactors of ILK. - and β-tubulin, ch-TOG (XMAP215), and RUVBL1 associate with ILK and colocalize with it to mitotic centrosomes. Inhibition of ILK activity or expression induces profound apoptosis-independent defects in the organization of the mitotic spindle and DNA segregation. ILK fails to localize to the centrosomes of abnormal spindles in RUVBL1-depleted cells. Additionally, depletion of ILK expression or inhibition of its activity inhibits Aurora A–TACC3/ch-TOG interactions, which are essential for spindle pole organization and mitosis. These data demonstrate a critical and unexpected function for ILK in the organization of centrosomal protein complexes during mitotic spindle assembly and DNA segregation.

A.B. Fielding and I. Dobreva contributed equally to this paper.

Abbreviations used in this paper: ILK, integrin-linked kinase; MTOC, microtubule organizing center; SILAC, stable isotope labeling with amino acids in cell culture.

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