Cdk and the anillin homolog Bud4 define a new pathway regulating septin organization in yeast

Eluère, Raïssa; Varlet, Isabelle; Bernadac, Alain; Simon, Marie‐Noëlle

doi:10.4161/cc.11.1.18542

Cited by 35 publications

(48 citation statements)

References 40 publications

(54 reference statements)

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“…2Ab, time 13-21), although little defect was evident until the end of mitosis. These results suggest that septins fail to maintain the intact ring structure in the absence of Bud4 during/after cytokinesis, consistent with recent reports (Eluère et al, 2012;Wloka et al, 2011).…”

Section: Resultssupporting

confidence: 82%

“…Although Bud4 is necessary for the integrity of the septin ring particularly during/after cytokinesis (this study; Eluère et al, 2012;Wloka et al, 2011), similar to Mid2 in S. pombe (Berlin et al, 2003;Tasto et al, 2003), our findings indicate that the anillin-related region of Bud4 is important for the assembly of the axial landmark. Bud4 might be a specialized anillin-related protein that coordinates cytokinesis and selection of a growth site, as these two processes are closely linked in haploid budding yeast (see below).…”

Section: Duf1709 and Ph Domains Of Bud4 Are Necessary For The Assemblmentioning

confidence: 73%

“…Bud4 then mediates the assembly of the axial landmark via DUF1709 and the PH domain (Kang et al, 2012; this study). Bud4 is also necessary for the integrity of the septin ring during and after cytokinesis (this study; Eluère et al, 2012;Wloka et al, 2011). The stable anchoring of both the septin and Bud4 rings at the division site depends on the interaction between Bud3 and the Cterminal domains of Bud4 and is likely to contribute to the fidelity of the axial budding pattern (this study).…”

Section: Role Of Bud4 In Linking Septins To the Axial Landmarkmentioning

confidence: 99%

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Coupling of septins to the axial landmark by Bud4 in budding yeast

Kang

Hood-DeGrenier

Park

2013

Journal of Cell Science

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SummaryCells of the budding yeast Saccharomyces cerevisiae select a site for polarized growth in a specific pattern that depends on their cell type. Haploid a and a cells bud in the axial budding pattern, which requires assembly of a landmark that includes the Bud4 protein. To understand how an axial bud site is established, we performed a structure-function analysis of Bud4. Bud4 contains DUF1709 (domain of unknown function), which is similar to a part of the anillin-homology domain, and a putative Pleckstrin homology (PH) domain near to its C terminus. Although its localization depends on septins, a conserved family of GTP-binding proteins, Bud4 is necessary for the stable inheritance of septin rings during cell division. Although some anillins interact directly with septins, we find that neither DUF1709 nor the PH domain is necessary for targeting Bud4 to the mother-bud neck. Instead, this C-terminal region is crucial for association of Bud4 with Bud3 and other components of the axial landmark. Remarkably, septins colocalize with Bud4 mutant proteins that lack these C-terminal domains, forming an arc or a single ring instead of a double ring during and after cytokinesis. Interestingly, overexpression of Bud4 also induces formation of extra Bud4 rings and arcs that are associated with septins. Analyses of a series of bud4 truncation mutants suggest that at least two domains in the central region play a redundant role in targeting Bud4 to the mother-bud neck and are thus likely to interact with septins. Taken together, these results indicate that Bud4 functions as a platform that links septins to the axial landmark.

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Section: Resultssupporting

confidence: 82%

Section: Duf1709 and Ph Domains Of Bud4 Are Necessary For The Assemblmentioning

confidence: 73%

Section: Role Of Bud4 In Linking Septins To the Axial Landmarkmentioning

confidence: 99%

See 1 more Smart Citation

Coupling of septins to the axial landmark by Bud4 in budding yeast

Kang

Hood-DeGrenier

Park

2013

Journal of Cell Science

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“…Not much is known about the roles of septin-binding proteins in yeast although polymerization of the septins into ring-like structures, the splitting of these rings shortly before cytokinesis and the formation of a septin-based diffusion barrier might necessitate similar activities (Qiu et al, 2008;Eluère et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Septin rings act as template for myosin higher-order structures and inhibit redundant polarity establishment

Schneider

Grois

Renz

et al. 2013

Journal of Cell Science

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SummaryThe mechanisms of the coordinated assembly and disassembly of the septin/myosin ring is central for the understanding of polar growth and cytokinesis in yeast and other organisms. The septin-and myosin-binding protein Bni5p provides a dual function during the formation and disassembly of septin/myosin rings. Early in the cell cycle, Bni5p captures Myo1p at the incipient bud site and actively transforms it into higher-order structures. Additionally, Bni5p stabilizes the septin/myosin ring and is released from the septins shortly before the onset of cytokinesis. If this Bni5p dissociation from the septins is artificially prevented, ring disassembly is impaired and the untimely appearance of septin/myosin ring is induced. The prematurely formed septin/myosin rings delay the establishment of a new polarity axis and the progression into a new cell cycle. This observation suggests a negative feedback between septin/myosin ring formation and polarity establishment that might help to guarantee the singular assembly of this structure and the synchronization of its formation with the cell cycle.

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“…Apart from bud site selection, Bud4 is known to play a role in septin organization, as the septins in bud4⌬ cells fail to form a discrete double ring during cytokinesis (21)(22)(23), whereas overexpression of Bud4 causes the assembly of extra septin structures (23). Bud4 is also required for normal cytokinesis in the absence of Gin4 or Cla4 (22), two protein kinases important for septin ring assembly (14).…”

mentioning

confidence: 99%

The Anillin-Related Region of Bud4 Is the Major Functional Determinant for Bud4's Function in Septin Organization during Bud Growth and Axial Bud Site Selection in Budding Yeast

Guo

Zhou

et al. 2015

Eukaryot Cell

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bThe anillin-related protein Bud4 of Saccharomyces cerevisiae is required for axial bud site selection by linking the axial landmark to the septins, which localize at the mother bud neck. Recent studies indicate that Bud4 plays a role in septin organization during cytokinesis. Here we show that Bud4 is also involved in septin organization during bud growth prior to cytokinesis, as bud4⌬ shs1⌬ cells displayed an elongated bud morphology and defective septin organization at 18°C. Bud4 overexpression also affected septin organization during bud growth in shs1⌬ cells at 30°C. Bud4 was previously thought to associate with the septins via its central region, while the C-terminal anillin-related region was not involved in septin association. Surprisingly, we found that the central region of Bud4 alone targets to the bud neck throughout the cell cycle, unlike full-length Bud4, which localizes to the bud neck only during G 2 /M phase. We identified the anillin-related region to be a second targeting domain that cooperates with the central region for proper septin association. In addition, the anillin-related region could largely mediate Bud4's function in septin organization during bud growth and bud site selection. We show that this region interacts with the C terminus of Bud3 and the two segments depend on each other for association with the septins. Moreover, like the bud4⌬ mutant, the bud3⌬ mutant genetically interacts with shs1⌬ and cdc12-6 mutants in septin organization, suggesting that Bud4 and Bud3 may cooperate in septin organization during bud growth. These observations provide new insights into the interaction of Bud4 with the septins and Bud3.

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Cdk and the anillin homolog Bud4 define a new pathway regulating septin organization in yeast

Cited by 35 publications

References 40 publications

Coupling of septins to the axial landmark by Bud4 in budding yeast

Coupling of septins to the axial landmark by Bud4 in budding yeast

Septin rings act as template for myosin higher-order structures and inhibit redundant polarity establishment

The Anillin-Related Region of Bud4 Is the Major Functional Determinant for Bud4's Function in Septin Organization during Bud Growth and Axial Bud Site Selection in Budding Yeast

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