Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end–binding microtubule destabilizer

Breugel, M. van; Drechsel, David; Hyman, Anthony

doi:10.1083/jcb.200211097

Cited by 115 publications

(128 citation statements)

References 44 publications

(79 reference statements)

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“…We could not confirm earlier results showing that Stu2 inhibits, rather than promotes, elongation of mammalian brain microtubules (12). Although Stu2 is a weak polymerase in the presence of porcine brain tubulin and requires high Stu2 concentrations, it nevertheless promoted microtubule growth under all conditions that we tested.…”

Section: Discussioncontrasting

confidence: 53%

“…Mutants lacking the TOG1 domain of Stu2 exhibit shorter cytoplasmic microtubules and shorter spindles (11), consistent with Stu2 promoting microtubule growth. However, studies with purified Stu2 have shown that it slows, rather than accelerates, elongation of microtubules grown in brain tubulin (12). Furthermore, these authors reported that Stu2 also promotes catastrophe, the transition of growing microtubules to shrinking ones, which often correlates with slower growth rates.…”

mentioning

confidence: 98%

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Stu2, the Budding Yeast XMAP215/Dis1 Homolog, Promotes Assembly of Yeast Microtubules by Increasing Growth Rate and Decreasing Catastrophe Frequency

Podolski

Mahamdeh

Howard

2014

Journal of Biological Chemistry

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Background:The reported inhibition of microtubule growth by Stu2 is difficult to reconcile with its cellular phenotypes. Results: Using microscopy assays, we found that Stu2 increases the growth rate and decreases the catastrophe frequency of yeast microtubules. Conclusion: Stu2 promotes microtubule growth, with considerably higher activity on budding yeast microtubules. Significance: The biochemical properties of Stu2 reported here account for the mitotic phenotypes observed in cells.

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Section: Discussioncontrasting

confidence: 53%

mentioning

confidence: 98%

Stu2, the Budding Yeast XMAP215/Dis1 Homolog, Promotes Assembly of Yeast Microtubules by Increasing Growth Rate and Decreasing Catastrophe Frequency

Podolski

Mahamdeh

Howard

2014

Journal of Biological Chemistry

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“…In vivo depletion of Stu2 can induce less dynamic cytoplasmic microtubules, with suppression of rescue and catastrophe and increased pausing time (Kosco et al, 2001). In vitro analysis, however, indicates that Stu2 acts primarily to destabilize microtubules (van Breugel et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

MOR1, theArabidopsis thalianahomologue ofXenopusMAP215, promotes rapid growth and shrinkage, and suppresses the pausing of microtubules in vivo

Kawamura

Wasteneys

2008

Journal of Cell Science

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MOR1, the Arabidopsis thaliana homologue of the Xenopus microtubule-associated protein MAP215, is required for spatial organization of the acentrosomal microtubule arrays of plant cells. To determine how loss of MOR1 function affects microtubule dynamics, we compared various parameters of microtubule dynamics in the temperature-sensitive mor1-1 mutant at its permissive and restrictive temperatures, 21°C and 31°C, respectively. Dynamic events were tracked in live cells expressing either GFP-tagged β-tubulin or the plus end tracking EB1. Microtubule growth and shrinkage velocities were both dramatically reduced in mor1-1 at 31°C and the incidence and duration of pause events increased. Interestingly, the association of EB1 with microtubule plus ends was reduced in mor1-1 whereas side wall binding increased, suggesting that MOR1 influences the association of EB1 with microtubules either by modulating microtubule plus end structure or by interacting with EB1. Although mor1-1 microtubules grew and shrank more slowly than wild-type microtubules at 21°C, the incidence of pause was not altered, suggesting that pause events, which occur more frequently at 31°C, have a major detrimental role in the spatial organization of cortical microtubules. Extensive increases in microtubule dynamics in wild-type cells when shifted from 21°C to 31°C underline the importance of careful temperature control in live cell imaging.

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“…Originally identified as a growth-promoting factor in Xenopus egg extracts (Gard and Kirschner, 1987), XMAP215 and related proteins are thought to favor polymerization of microtubules, although XMAP215 itself and its S. cerevisiae homologue Stu2p can also promote microtubule depolymerization (Shirasu-Hiza et al, 2003;van Breugel et al, 2003). In C. elegans embryos, the XMAP215 homologue ZYG-9 is present in the cytoplasm and enriched at centrosomes throughout the cell cycle (Matthews et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

ZYG-9, TAC-1 and ZYG-8 together ensure correct microtubule function throughout the cell cycle of C. elegans embryos

Bellanger

Carter

Phillips

et al. 2007

Journal of Cell Science

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The early Caenorhabditis elegans embryo is well suited for investigating microtubule-dependent cell division processes. In the one-cell stage, the XMAP215 homologue ZYG-9, associated with the TACC protein TAC-1, promotes microtubule growth during interphase and mitosis, whereas the doublecortin domain protein ZYG-8 is required for anaphase spindle positioning. How ZYG-9, TAC-1 and ZYG-8 together ensure correct microtubule-dependent processes throughout the cell cycle is not fully understood. Here, we identify new temperature-sensitive alleles of zyg-9 and tac-1. Analysis of ZYG-9 and TAC-1 distribution in these mutants identifies amino acids important for centrosomal targeting and for stability of the two proteins. This analysis also reveals that TAC-1 is needed for correct ZYG-9 centrosomal enrichment. Moreover, we find that ZYG-9, but not TAC-1, is limiting for microtubule-dependent processes in one-cell-stage embryos. Using two of these alleles to rapidly inactivate ZYG-9-TAC-1 function, we establish that this complex is required for correct anaphase spindle positioning. Furthermore, we uncover that ZYG-9-TAC-1 and ZYG-8 function together during meiosis, interphase and mitosis. We also find that TAC-1 physically interacts with ZYG-8 through its doublecortin domain, and that in vivo TAC-1 and ZYG-8 are part of a complex that does not contain ZYG-9. Taken together, these findings indicate that ZYG-9-TAC-1 and ZYG-8 act in a partially redundant manner to ensure correct microtubule assembly throughout the cell cycle of early C. elegans embryos.

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Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end–binding microtubule destabilizer

Cited by 115 publications

References 44 publications

Stu2, the Budding Yeast XMAP215/Dis1 Homolog, Promotes Assembly of Yeast Microtubules by Increasing Growth Rate and Decreasing Catastrophe Frequency

Stu2, the Budding Yeast XMAP215/Dis1 Homolog, Promotes Assembly of Yeast Microtubules by Increasing Growth Rate and Decreasing Catastrophe Frequency

MOR1, theArabidopsis thalianahomologue ofXenopusMAP215, promotes rapid growth and shrinkage, and suppresses the pausing of microtubules in vivo

ZYG-9, TAC-1 and ZYG-8 together ensure correct microtubule function throughout the cell cycle of C. elegans embryos

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