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Journal of Cell Science 115, 3389-3402 (2002)
© 2002 The Company of Biologists Limited

Research Article

A novel centrosome-associated protein with affinity for microtubules

Pascal A. Stein1, Christopher P. Toret1, Adrian N. Salic2, Melissa M. Rolls1 and Tom A. Rapoport1,*

1 Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115-6091, USA
2 Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115-6091, USA

* Author for correspondence (e-mail: tom_rapoport{at}hms.harvard.edu)

Accepted 12 June 2002

We have identified a novel mammalian protein, MIR1, with microtubule-binding activity. MIR1 is a relative of MID1/midin, the protein implicated in Opitz G/BBB syndrome. In tissue culture cells, MIR1 is enriched at the centrosome. MIR1 dissociates from centrosomes at the G2/M transition and is recruited back to spindle poles during anaphase. When overexpressed during interphase, MIR1 binds along microtubule filaments, which become stabilized, bundled and detached from the centrosome. In mitosis, overexpressed MIR1 dissociates from microtubules but still affects the normally focused localization of {gamma}-tubulin in spindle poles. Tight binding to microtubules in interphase appears to require an oligomeric state of MIR1, and phosphorylation in mitosis at predicted cyclin-dependent kinase (cdk) sites weakens the interaction.

Key words: Microtubule, Centrosome, Phosphorylation, Cell cycle


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© The Company of Biologists Ltd 2002