The p150-Glued Ssm4p regulates microtubular dynamics and nuclear movement in fission yeast

Niccoli, Teresa; Yamashita, Akira; Nurse, Paul; Yamamoto, Masayuki

doi:10.1242/jcs.01475

Cited by 42 publications

(77 citation statements)

References 65 publications

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“…The CAP-Gly-containing proteins are crucial for astral MT interactions with cortical dynein-dynactin patches during mitosis and for the delivery of motors such as dynein to their site of action (Coquelle et al, 2002;Lansbergen et al, 2004;Niccoli et al, 2004;Tai et al, 2002;Vaughan et al, 2002;Xiang et al, 2000). In budding yeast, dynein is delivered to the cortex on the plus ends of polymerizing MTs.…”

Section: Introductionmentioning

confidence: 99%

A new role for kinesin-directed transport of Bik1p (CLIP-170) in Saccharomyces cerevisiae

Caudron

Andrieux

Job

et al. 2008

Journal of Cell Science

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Bik1p is the budding yeast counterpart of the CLIP-170 family of microtubule plus-end tracking proteins, which are required for dynein localization at plus ends and dynein-dependent spindle positioning. CLIP-170 proteins make up a CAP-Gly microtubule-binding domain, which sustains their microtubule plus-end tracking behaviour. However, in yeast, Bik1p travels towards plus ends as a cargo of the plus-end-directed kinesin Kip2p. Additionally, Kip2p behaves as a plus-end-tracking protein; hence, it has been proposed that Bik1p might track plus ends principally as a cargo of Kip2p. Here, we examined Bik1p localization in yeast strains expressing mutant tubulin lacking the C-terminal amino acid (Glu tubulin; lacking Phe), the interaction of which with Bik1p is severely impaired compared with wild type. In Glu-tubulin strains, despite the presence of robust Kip2p comets at microtubule plus ends, Bik1p failed to track plus ends. Despite Bik1p depletion at plus ends, dynein positioning at the same plus ends was unperturbed. Video microscopy and genetic evidence indicated that dynein was transported at plus ends in a Kip2p-Bik1p-dependent manner, and was then capable of tracking Bik1p-depleted plus ends. These results indicate that Bik1p interactions with tubulin are important for Bik1p plus-end tracking, and suggest alternative pathways for Bik1p-Kip2p-dependent dynein localization at plus ends.

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Section: Introductionmentioning

confidence: 99%

A new role for kinesin-directed transport of Bik1p (CLIP-170) in Saccharomyces cerevisiae

Caudron

Andrieux

Job

et al. 2008

Journal of Cell Science

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“…Another group of SPB proteins has been identified based on their specific requirement during meiosis. Among these proteins are Hrs1/Mcp6, a coiled-coiled protein produced specifically during meiosis (Saito et al, 2005;Tanaka et al, 2005), and Ssm4 (Niccoli et al, 2004), a p150-Glued protein, which are both required for horsetail nuclear movement and recombination of sister chromosomes, and Spo15, a meiotic coiled-coil SPB protein involved in spore membrane formation (Ikemoto et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Ppc89 Links Multiple Proteins, Including the Septation Initiation Network, to the Core of the Fission Yeast Spindle-Pole Body

Rosenberg

Tomlin

McDonald

et al. 2006

MBoC

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The spindle-pole body (SPB), the yeast analog of the centrosome, serves as the major microtubule (MT) organizing center in the yeast cell. In addition to this central function, the SPB organizes and concentrates proteins required for proper coordination between the nuclear-division cycle and cytokinesis. For example, the Schizosaccharomyces pombe septationinitiation network (SIN), which is responsible for initiating actomyosin ring constriction and septation, is assembled at the SPB through its two scaffolding components, Sid4 and Cdc11. In an effort to identify novel SIN interactors, we purified Cdc11 and identified by mass spectrometry a previously uncharacterized protein associated with it, Ppc89. Ppc89 localizes constitutively to the SPB and interacts directly with Sid4. A fusion between the N-terminal 300 amino acids of Sid4 and a SPB targeting domain of Ppc89 supplies the essential function of Sid4 in anchoring the SIN. ppc89⌬ cells are inviable and exhibit defects in SPB integrity, and hence in spindle formation, chromosome segregation, and SIN localization. Ppc89 overproduction is lethal, resulting primarily in a G2 arrest accompanied by massive enlargement of the SPB and increased SPB MT nucleation. These results suggest a fundamental role for Ppc89 in organization of the S. pombe SPB.

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“…Glued regulates microtubule dynamics (Niccoli et al, 2004). In human cells, this regulation depends on association with EB1 and is essential to maintain the radial arrays of microtubules in interphase cells (Askham et al, 2002;Strickland et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Dynactin targets Pavarotti-KLP to the central spindle during anaphase and facilitates cytokinesis inDrosophilaS2 cells

Delcros

Prigent

Giet

2006

Journal of Cell Science

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The dynactin complex cooperates with the dynein complex in various systems for mitotic completion. Here we analysed the mitotic phenotype of Drosophila S2 cells following the knockdown of the dynactin subunit p150Glued. We found that p150Glued-depleted cells were delayed in metaphase and that the centrosomes were poorly connected to mitotic spindle poles. In addition, anaphase occurred with asynchronous chromosome segregation. Although cyclin B was degraded in these anaphase cells, Aurora B, MEI-S322 and BubR1 were not released from the non-segregating chromosomes. We also found that the density and organisation of the central spindle were compromised, with Aurora B and polo kinases absent from the diminished number of microtubules. Pavarotti-KLP, a component of the centralspindlin complex required for the formation of stable microtubule bundles, was not immediately targeted to the plus ends of the microtubules following anaphase onset as happened in controls. Instead, it accumulated transiently at the cell cortex during early anaphase and its targeting to the central spindle was delayed. These data suggest that the dynactin complex contributes to cytokinesis by promoting stable targeting of the centralspindlin complex to microtubule plus ends at anaphase onset. The contribution of the dynein-dynactin complex to synchronous chromosome segregation and cytokinesis is discussed.

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The p150-Glued Ssm4p regulates microtubular dynamics and nuclear movement in fission yeast

Cited by 42 publications

References 65 publications

A new role for kinesin-directed transport of Bik1p (CLIP-170) in Saccharomyces cerevisiae

A new role for kinesin-directed transport of Bik1p (CLIP-170) in Saccharomyces cerevisiae

Ppc89 Links Multiple Proteins, Including the Septation Initiation Network, to the Core of the Fission Yeast Spindle-Pole Body

Dynactin targets Pavarotti-KLP to the central spindle during anaphase and facilitates cytokinesis inDrosophilaS2 cells

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