ArticleMolecular biology of the cell2019
The J-domain cochaperone Rsp1 interacts with Mto1 to organize noncentrosomal microtubule assembly.
Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Noncentrosomal Microtubule Assembly and Its Regulation.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Klp2-mediated Rsp1-Mto1 colocalization inhibits microtubule-dependent microtubule assembly in fission yeast.Science advances · 2025Article
- Reliable and robust control of nucleus centering is contingent on nonequilibrium force patterns.iScience · 2023Article
- Fission yeast cells mix parental mitochondria in a progressive manner during meiosis.Journal of molecular cell biology · 2023Article
- Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex.Nature communications · 2021Article
- Klp2 and Ase1 synergize to maintain meiotic spindle stability during metaphase I.The Journal of biological chemistry · 2020Article
- Alp7-Mto1 and Alp14 synergize to promote interphase microtubule regrowth from the nuclear envelope.Journal of molecular cell biology · 2019Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubule biogenesis initiates at various intracellular sites, including the centrosome, the Golgi apparatus, the nuclear envelope, and preexisting microtubules. Similarly, in the fission yeast Schizosaccharomyces pombe, interphase microtubules are nucleated at the spindle pole body (SPB), the nuclear envelope, and preexisting microtubules, depending on Mto1 activity. Despite the essential role of Mto1 in promoting microtubule nucleation, how distribution of Mto1 in different sites is regulated has remained elusive. Here, we show that the J-domain cochaperone Rsp1 interacts with Mto1 and specifies the localization of Mto1 to non-SPB nucleation sites. The absence of Rsp1 abolishes the localization of Mto1 to non-SPB nucleation sites, with concomitant enrichment of Mto1 to the SPB and the nuclear envelope. In contrast, Rsp1 overexpression impairs the localization of Mto1 to all microtubule organization sites. These findings delineate a previously uncharacterized mechanism in which Rsp1-Mto1 interaction orchestrates non-SPB microtubule formation.
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