Septin mutations and phenotypes in <i>S. cerevisiae</i>

Mela, Alexander; Momany, Michelle

doi:10.1002/cm.21492

Cited by 9 publications

(5 citation statements)

References 45 publications

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“…Interaction partners previously identified suggested a role for SEPT9 in vesicle transport to and from the plasma membrane [93]. The other three core septins (Cdc3, Cdc11 and Cdc12) are encoded by essential genes and therefore the null mutants cannot be interrogated [94]. Whether the involvement of Cdc10 (or potentially other septins) in CoQ6 uptake/transport is related to the role of septins in endocytosis or a different septin function, will require further experimentation.…”

Section: Discussionmentioning

confidence: 99%

Genes and lipids that impact uptake and assimilation of exogenous coenzyme Q in Saccharomyces cerevisiae

Fernández-del-Rio

Kelly

Contreras

et al. 2020

Free Radical Biology and Medicine

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ORFΔcoq2Δ, yeast double mutant harboring a gene deletion in a designated open reading frame plus a deletion in COQ2; pABA, para-aminobenzoic acid; PC, phosphatidylcholine; Pyr12, 1-pyrene dodecanoic acid; SD, synthetic dextrose medium; vCLAMP, vacuole-mitochondria patch; WT, wild-type parental yeast strain; YPD, rich growth medium containing dextrose as a fermentable carbon source; YPG, rich growth medium contain glycerol as the sole non-fermentable carbon source.

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Section: Discussionmentioning

confidence: 99%

Genes and lipids that impact uptake and assimilation of exogenous coenzyme Q in Saccharomyces cerevisiae

Fernández-del-Rio

Kelly

Contreras

et al. 2020

Free Radical Biology and Medicine

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“…Septins and anillin are cytoskeletal-binding proteins essential for cytokinesis in some, but not all, cell types and model systems; their precise roles in cytokinesis remain unclear. [51][52][53] The septins are essential for cytokinesis in budding yeast 54,55 but are not required for cytokinesis in other cell types, including in S. pombe 56 , mouse myeloid and lymphoid hematopoietic cells 25 , and mouse neuronal precursor cells 57 . And, in cultured mammary epithelial cells, septin-6 expression is inversely correlated with successful cytokinesis, suggesting an inhibitory role.…”

Section: Introductionmentioning

confidence: 99%

Germ fate determinants protect germ precursor cell division by restricting septin and anillin levels at the division plane

Connors,

Mauro,

Tristian Wiles

et al. 2023

Preprint

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SummaryAnimal cell cytokinesis, or the physical division of one cell into two, is thought to be driven by constriction of an actomyosin contractile ring at the division plane. The mechanisms underlying cell type-specific differences in cytokinesis remain unknown. Germ cells are totipotent cells that pass genetic information to the next generation. Previously, usingformincyk-1(ts)mutantC. elegansembryos, we found that the P2 germ precursor cell is protected from cytokinesis failure and can divide without detectable F-actin at the division plane. Here, we identified two canonical germ fate determinants required for P2-specific cytokinetic protection: PIE-1 and POS-1. Neither has been implicated previously in cytokinesis. These germ fate determinants protect P2 cytokinesis by reducing the accumulation of septinUNC-59and anillinANI-1at the division plane, which here act as negative regulators of cytokinesis. These findings may provide insight into cytokinetic regulation in other cell types, especially in stem cells with high potency.

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“…Second, relevant scaffold proteins, which provide functions such as binding and supporting protein interactions, are transported to the division site to assist with the assembly of the actin ring (GE AND BALASUBRAMANIAN 2008;LI et al 2016). Third, a contractile actin ring composed of actin, septin and formin is formed (COURTEMANCHE 2018;MELA AND MOMANY 2019). This step is regulated by a conserved signaling kinase cascade, such as the septation-initiation network (SIN) in Saccharomyces pombe and the mitotic-exit network (MEN) in the budding yeast Saccharomyces cerevisiae (MULVIHILL et al 2001;CORBETT et al 2006).…”

Section: Introductionmentioning

confidence: 99%

The Scaffold Proteins Paxillin B and α-Actinin Regulate Septation in Aspergillus nidulans via Control of Actin Ring Contraction

et al. 2020

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Cytokinesis, as the final step of cell division, plays an important role in fungal growth and proliferation. In the filamentous fungus Aspergillus nidulans, defective cytokinesis is able to induce abnormal multinuclear or nonnucleated cells and then result in reduced hyphal growth and abolished sporulation. Previous studies have reported that a conserved contractile actin ring (CAR) protein complex and the septation initiation network (SIN) signaling kinase cascade are required for cytokinesis and septation; however, little is known about the role(s) of scaffold proteins involved in these two important cellular processes. In this study, we show that a septum-localized scaffold protein paxillin B (PaxB) is essential for cytokinesis/septation in A. nidulans. The septation defects observed in a paxB deletion strain resemble those caused by the absence of another identified scaffold protein, α-actinin (AcnA). Deletion of α-actinin (AcnA) leads to undetectable PaxB at the septation site, whereas deletion of paxB does not affect the localization of α-actinin at septa. However, deletion of either α-actinin (acnA) or paxB causes the actin ring to disappear at septation sites during cytokinesis. Notably, overexpression of α-actinin acnA partially rescues the septum defects of the paxB mutant but not vice versa, suggesting AcnA may play a dominant role over that of PaxB for cytokinesis and septation. In addition, PaxB and α-actinin affect the septal dynamic localization of MobA, a conserved component of the SIN pathway, suggesting they may affect the SIN protein complex function at septa. Protein pull-down assays combined with liquid chromatography–mass spectrometry identification indicate that α-actinin AcnA and PaxB likely do not directly interact, but presumably belong to an actin cytoskeleton protein network that is required for the assembly and contraction of the CAR. Taken together, findings in this study provide novel insights into the roles of conserved scaffold proteins during fungal septation in A. nidulans.

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Septin mutations and phenotypes in S. cerevisiae

Cited by 9 publications

References 45 publications

Genes and lipids that impact uptake and assimilation of exogenous coenzyme Q in Saccharomyces cerevisiae

Genes and lipids that impact uptake and assimilation of exogenous coenzyme Q in Saccharomyces cerevisiae

Germ fate determinants protect germ precursor cell division by restricting septin and anillin levels at the division plane

The Scaffold Proteins Paxillin B and α-Actinin Regulate Septation in Aspergillus nidulans via Control of Actin Ring Contraction

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