A novel centrosome-associated protein with affinity for microtubules | Zendy

Pascal A. Stein | Zendy; Christopher P. Toret | Zendy; Adrian Salic | Zendy; Melissa M. Rolls | Zendy; Tom A. Rapoport | Zendy

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A novel centrosome-associated protein with affinity for microtubules

Author(s) -

Pascal A. Stein,

Christopher P. Toret,

Adrian Salic,

Melissa M. Rolls,

Tom A. Rapoport

Publication year - 2002

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.115.17.3389

Subject(s) - centrosome , biology , anaphase , microbiology and biotechnology , microtubule , mitosis , interphase , microtubule organizing center , microtubule nucleation , cyclin dependent kinase , spindle pole body , astral microtubules , spindle apparatus , genetics , cell cycle , cell division , gene , cell

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.

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