A novel centrosome-associated protein with affinity for microtubules

Pascal A. Stein, Christopher P. Toret, Adrian N. Salic, Melissa Rolls, Tom A. Rapoport

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


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 γ-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.

Original languageEnglish (US)
Pages (from-to)3389-3402
Number of pages14
JournalJournal of Cell Science
Issue number17
StatePublished - Sep 1 2002

All Science Journal Classification (ASJC) codes

  • Cell Biology


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