Rho1- and Pkc1-dependent phosphorylation of the F-BAR protein Syp1 contributes to septin ring assembly

Merlini, Laura; Bolognesi, Alessio; Juanes, M. Angeles; Vandermoere, Franck; Courtellemont, Thibault; Pascolutti, Roberta; Séveno, Martial; Barral, Yves; Piatti, Simonetta

doi:10.1091/mbc.e15-06-0366

Cited by 21 publications

(24 citation statements)

References 130 publications

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“…In agreement with this conclusion, expression of a hyperactive variant of Bni1 (BNI1-V360D) (KONO et al 2012) restored robust actin cables and rescued the sensitivity to LatB of dma1D dma2D cells (Figure 3, E and F), whereas it did not suppress their temperature sensitivity ( Figure 3G). Furthermore, BNI1-V360D did not suppress the temperature sensitivity of dma1D dma2D cla4-75 cells ( Figure S5) that we mainly ascribed to defects in septin organization (Merlini et al 2012(Merlini et al , 2015. Thus, formins likely act downstream of Dma proteins in the control of cell polarization.…”

Section: Resultsmentioning

confidence: 90%

“…Remarkably, we find that the spindle positioning defects of dma1 dma2 mutant cells are also partially suppressed by expression of the hyperactive Bni1-V360D variant, suggesting that they are partly caused by a sluggish actin cable network. In contrast, Bni1-V360D does not rescue the lethality of dma1 dma2 cla4 triple mutant cells that was primarily attributed to septin defects (Merlini et al 2012(Merlini et al , 2015. …”

Section: Formin Regulation By Dma Ubiquitin Ligases 213mentioning

confidence: 82%

“…We recently showed that hyperactivation of the Rho1 GTPase and its effector protein kinase C (Pkc1) recue the temperature sensitivity and septin defects of dma1D dma2D cla4-75 triple mutant cells (Merlini et al 2015). Since Rho1 and Pkc1 are known formin regulators together with Cdc42 (Kohno et al 1996;Evangelista et al 1997;Imamura et al 1997;Dong et al 2003), we asked if hyperactivation of these proteins could rescue the mislocalization of Bni1 and impaired actin cable organization of dma1D dma2D double mutant cells.…”

Section: Dma1 and Dma2 Are Required For Proper Formin Localizationmentioning

confidence: 99%

“…Since Rho1 and Pkc1 are known formin regulators together with Cdc42 (Kohno et al 1996;Evangelista et al 1997;Imamura et al 1997;Dong et al 2003), we asked if hyperactivation of these proteins could rescue the mislocalization of Bni1 and impaired actin cable organization of dma1D dma2D double mutant cells. To address this question, we used the dominant hyperactive alleles RHO1-D72N (Merlini et al 2015), PKC1-R398P (Nonaka et al 1995), and CDC42-D65N (Mosch et al 2001). None of these mutant alleles restored normal Bni1 localization ( Figure 6A), sensitivity to LatB (Figure 6B), or robust actin cable organization ( Figure 6C) in dma1D dma2D cells, suggesting that the polarity defects of this mutant are probably unlinked to a reduced activity of the above factors.…”

Section: Dma1 and Dma2 Are Required For Proper Formin Localizationmentioning

confidence: 99%

“…Interestingly, expression of the hyperactive Bni1-V360V protein partially, but significantly, decreased the average spindle distance from the bud neck in dma1D dma2D mutant cells (1.3 6 1.1 mm, n = 108 in dma1D dma2D BNI1-V360D cells vs. 1.6 6 1.2 mm, n = 124 in dma1D dma2D cells, Figure 5D). Thus, inefficient spindle positioning in dma1D dma2D cells is likely due to both Elm1 and formin localization defects.Hyperactivation of Rho1, Cdc42, or Pkc1, as well as GIC2 overexpression, do not restore proper Bni1 localization and actin cable network in dma1D dma2D cellsWe recently showed that hyperactivation of the Rho1 GTPase and its effector protein kinase C (Pkc1) recue the temperature sensitivity and septin defects of dma1D dma2D cla4-75 triple mutant cells (Merlini et al 2015). Since Rho1 and Pkc1 are known formin regulators together with Cdc42 (Kohno et al 1996;Evangelista et al 1997;Imamura et al 1997;Dong et al 2003), we asked if hyperactivation of these proteins could rescue the mislocalization of Bni1 and impaired actin cable organization of dma1D dma2D double mutant cells.…”

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Control of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2

Juanes¹,

Piatti²

2016

Genetics

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Formins are widespread actin-polymerizing proteins that play pivotal roles in a number of processes, such as cell polarity, morphogenesis, cytokinesis, and cell migration. In agreement with their crucial function, formins are prone to a variety of regulatory mechanisms that include autoinhibition, post-translational modifications, and interaction with formin modulators. Furthermore, activation and function of formins is intimately linked to their ability to interact with membranes. In the budding yeast Saccharomyces cerevisiae, the two formins Bni1 and Bnr1 play both separate and overlapping functions in the organization of the actin cytoskeleton. In addition, they are controlled by both common and different regulatory mechanisms. Here we show that proper localization of both formins requires the redundant E3 ubiquitin ligases Dma1 and Dma2, which were previously involved in spindle positioning and septin organization. In dma1 dma2 double mutants, formin distribution at polarity sites is impaired, thus causing defects in the organization of the actin cable network and hypersensitivity to the actin depolymerizer latrunculin B. Expression of a hyperactive variant of Bni1 (Bni1-V360D) rescues these defects and partially restores proper spindle positioning in the mutant, suggesting that the failure of dma1 dma2 mutant cells to position the spindle is partly due to faulty formin activity. Strikingly, Dma1/2 interact physically with both formins, while their ubiquitin-ligase activity is required for formin function and polarized localization. Thus, ubiquitylation of formin or a formin interactor(s) could promote formin binding to membrane and its ability to nucleate actin. Altogether, our data highlight a novel level of formin regulation that further expands our knowledge of the complex and multilayered controls of these key cytoskeleton organizers. KEYWORDS actin; formin; ubiquitylation; budding yeast T HE ability to polarize is a fundamental property of all types of cells, being crucial for numerous cellular processes such as proliferation, differentiation, and morphogenesis. Indeed, dysregulation of cell polarity can underlie developmental disorders and cancers (Wodarz and Nathke 2007). Cell polarization is strictly linked to the reorganization of the cytoskeleton and in particular of the actin network, whose dynamics must be tightly controlled for polarized processes to occur properly.The unicellular budding yeast Saccharomyces cerevisiae divides asymmetrically and undergoes highly polarized cell growth throughout its life cycle. Most aspects of polarized growth in budding yeast arise from a precise arrangement of the cortical actin cytoskeleton during the cell cycle. Three main actin structures can be found in yeast cells: (i) actin patches, which are sites of active endocytosis, (ii) actin cables, which serve as tracks for polarized secretion and segregation of organelles, and (iii) the contractile acto-myosin ring, which is involved in cytokinesis (Adams and Pringle 1984;Kilmartin and Adams 1984;Bi et ...

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Section: Resultsmentioning

confidence: 90%

Section: Formin Regulation By Dma Ubiquitin Ligases 213mentioning

confidence: 82%

Section: Dma1 and Dma2 Are Required For Proper Formin Localizationmentioning

confidence: 99%

Section: Dma1 and Dma2 Are Required For Proper Formin Localizationmentioning

confidence: 99%

mentioning

confidence: 99%

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Control of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2

Juanes¹,

Piatti²

2016

Genetics

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The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae

Juanes

Piatti²

2016

Cell. Mol. Life Sci.

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Cell division is a fundamental but complex process that gives rise to two daughter cells. It includes an ordered set of events, altogether called “the cell cycle”, that culminate with cytokinesis, the final stage of mitosis leading to the physical separation of the two daughter cells. Symmetric cell division equally partitions cellular components between the two daughter cells, which are therefore identical to one another and often share the same fate. In many cases, however, cell division is asymmetrical and generates two daughter cells that differ in specific protein inheritance, cell size, or developmental potential. The budding yeast Saccharomyces cerevisiae has proven to be an excellent system to investigate the molecular mechanisms governing asymmetric cell division and cytokinesis. Budding yeast is highly polarized during the cell cycle and divides asymmetrically, producing two cells with distinct sizes and fates. Many components of the machinery establishing cell polarization during budding are relocalized to the division site (i.e., the bud neck) for cytokinesis. In this review we recapitulate how budding yeast cells undergo polarized processes at the bud neck for cell division.

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Protein kinase C is required for the pathogenicity of Setosphaeria turcica on maize

Sun

Dong

et al. 2023

J Plant Pathol

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Rho1- and Pkc1-dependent phosphorylation of the F-BAR protein Syp1 contributes to septin ring assembly

Cited by 21 publications

References 130 publications

Control of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2

Control of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2

The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae

Protein kinase C is required for the pathogenicity of Setosphaeria turcica on maize

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