Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of the γ-tubulin complex and directly interacts with GCP3Alp6

Deepsharan K. Dhani, Benjamin T. Goult, Gifty M. George, Daniel T. Rogerson, Danny A. Bitton, Crispin J. Miller, John W R Schwabe, Kayoko Tanaka

Research output: Contribution to journalArticlepeer-review

Abstract

In humans, MOZART1 plays an essential role in mitotic spindle formation as a component of the γ-tubulin ring complex. We report that the fission yeast homologue of MOZART1, Mzt1/Tam4, is located at microtubule-organizing centers (MTOCs) and coimmunoprecipitates with γ-tubulin Gtb1 from cell extracts. We show that mzt1/tam4 is an essential gene in fission yeast, encoding a 64-amino acid peptide, depletion of which leads to aberrant microtubule structure, including malformed mitotic spindles and impaired interphase micro-tubule array. Mzt1/Tam4 depletion also causes cytokinesis defects, suggesting a role of the γ-tubulin complex in the regulation of cytokinesis. Yeast two-hybrid analysis shows that Mzt1/Tam4 forms a complex with Alp6, a fission yeast homologue of γ-tubulin complex protein 3 (GCP3). Biophysical methods demonstrate that there is a direct interaction between recombinant Mzt1/Tam4 and the N-terminal region of GCP3Alp6. Together our results suggest that Mzt1/Tam4 contributes to the MTOC function through regulation of GCP3Alp6. © 2013 Dhani et al.
Original languageEnglish
Pages (from-to)3337-3349
Number of pages12
JournalMolecular Biology of the Cell
Volume24
Issue number21
DOIs
Publication statusPublished - 1 Nov 2013

Research Beacons, Institutes and Platforms

  • Manchester Cancer Research Centre

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