scholarly journals The small GTPase Rho3 and the diaphanous/formin For3 function in polarized cell growth in fission yeast

2002 ◽  
Vol 115 (23) ◽  
pp. 4629-4639 ◽  
Author(s):  
K. Nakano
Keyword(s):  
Cell Growth ◽  
Fission Yeast ◽  
Small Gtpase ◽  
Polarized Cell Growth

scholarly journals Cytokinesis-Based Constraints on Polarized Cell Growth in Fission Yeast

PLoS Genetics ◽  
2012 ◽  
Vol 8 (10) ◽  
pp. e1003004 ◽  
Author(s):  
K. Adam Bohnert ◽  
Kathleen L. Gould
Keyword(s):  
Cell Growth ◽  
Fission Yeast ◽  
Polarized Cell Growth

Cdc42 regulates polarized growth and cell integrity in fission yeast

2014 ◽  
Vol 42 (1) ◽  
pp. 201-205 ◽  
Author(s):  
Sergio A. Rincón ◽  
Miguel Estravís ◽  
Pilar Pérez
Keyword(s):  
Cell Growth ◽  
Fission Yeast ◽  
Rho Gtpase ◽  
Short Review ◽  
Model Systems ◽  
Polarized Growth ◽  
Cell Integrity ◽  
Polarized Cell Growth ◽  
New Material ◽  
High Level

Polarized cell growth requires a well-orchestrated number of events, namely selection of growth site, organization of cytoskeleton elements and delivery of new material to the growth region. The small Rho GTPase Cdc42 has emerged as a major organizer of polarized growth through its participation in many of these events. In the present short review, we focus on the regulation of Cdc42 activity and localization as well as how it controls downstream events necessary for polarized cell growth in Schizosaccharomyces pombe. Owing to the high level of similarity of the polarity pathways, analogies between fission yeast and other model systems can be useful to decipher how cells can actively define their shape by polarized growth.

scholarly journals The Conserved NDR Kinase Orb6 Controls Polarized Cell Growth by Spatial Regulation of the Small GTPase Cdc42

2009 ◽  
Vol 19 (15) ◽  
pp. 1314-1319 ◽  
Author(s):  
Maitreyi Das ◽  
David J. Wiley ◽  
Xi Chen ◽  
Kavita Shah ◽  
Fulvia Verde
Keyword(s):  
Cell Growth ◽  
Small Gtpase ◽  
Spatial Regulation ◽  
Polarized Cell Growth ◽  
Ndr Kinase

scholarly journals Regulation of the Formin for3p by cdc42p and bud6p

2007 ◽  
Vol 18 (10) ◽  
pp. 4155-4167 ◽  
Author(s):  
Sophie G. Martin ◽  
Sergio A. Rincón ◽  
Roshni Basu ◽  
Pilar Pérez ◽  
Fred Chang
Keyword(s):  
Cell Growth ◽  
Fission Yeast ◽  
Rho Gtpase ◽  
Intramolecular Interaction ◽  
Actin Cable ◽  
Polarized Cell Growth ◽  
N Terminus ◽  
Cable Assembly ◽  
Actin Cables

Formins are conserved actin nucleators responsible for the assembly of diverse actin structures. Many formins are controlled through an autoinhibitory mechanism involving the interaction of a C-terminal DAD sequence with an N-terminal DID sequence. Here, we show that the fission yeast formin for3p, which mediates actin cable assembly and polarized cell growth, is regulated by a similar autoinhibitory mechanism in vivo. Multiple sites govern for3p localization to cell tips. The localization and activity of for3p are inhibited by an intramolecular interaction of divergent DAD and DID-like sequences. A for3p DAD mutant expressed at endogenous levels produces more robust actin cables, which appear to have normal organization and dynamics. We identify cdc42p as the primary Rho GTPase involved in actin cable assembly and for3p regulation. Both cdc42p, which binds at the N terminus of for3p, and bud6p, which binds near the C-terminal DAD-like sequence, are needed for for3p localization and full activity, but a mutation in the for3p DAD restores for3p localization and other phenotypes of cdc42 and bud6 mutants. In particular, the for3p DAD mutation suppresses the bipolar growth (NETO) defect of bud6Δ cells. These findings suggest that cdc42p and bud6p activate for3p by relieving autoinhibition.

scholarly journals Activation of polarized cell growth by inhibition of cell polarity

2018 ◽  
Author(s):  
Marco Geymonat ◽  
Anatole Chessel ◽  
James Dodgson ◽  
Hannah Punter ◽  
Felix Horns ◽  
...  
Keyword(s):  
Cell Growth ◽  
Fission Yeast ◽  
Cell Polarity ◽  
Rho Gtpase ◽  
Dependent Manner ◽  
Polarized Cell Growth ◽  
And Control ◽  
Polarity Factor ◽  
Pak Kinase

AbstractA key feature of cells is the capacity to activate new functional polarized domains contemporaneously to pre-existing ones. How cells accomplish this is not clear. Here, we show that in fission yeast inhibition of cell polarity at pre-existing domains of polarized cell growth is required to activate new growth. This inhibition is mediated by the ERM-related polarity factor Tea3, which antagonizes the activation of the Rho-GTPase Cdc42 by its co-factor Scd2. We demonstrate that Tea3 acts in a phosphorylation-dependent manner controlled by the PAK kinase Shk1 and that, like Scd2, Tea3 is direct substrate of Shk1. Importantly, we show that Tea3 and Scd2 compete for their binding to Shk1, indicating that their biochemical competition for Shk1 underpins their antagonistic roles in controlling polarity. Thus, by preventing pre-existing growth domains from becoming overpowering, Tea3 allows cells to redistribute their polarity-activating machinery to prospective sites and control their timing of activation.

scholarly journals Activation of Cdc42 GTPase upon CRY2-Induced Cortical Recruitment Is Antagonized by GAPs in Fission Yeast

Cells ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 2089 ◽  
Author(s):  
Iker Lamas ◽  
Nathalie Weber ◽  
Sophie G. Martin
Keyword(s):  
Fission Yeast ◽  
Positive Feedback ◽  
Antagonistic Activity ◽  
Cell Polarization ◽  
Small Gtpase ◽  
Nucleotide Exchange ◽  
Gtpase Activating Protein ◽  
Guanine Nucleotide Exchange ◽  
Nucleotide Exchange Factor ◽  
Cell Architecture

The small GTPase Cdc42 is critical for cell polarization in eukaryotic cells. In rod-shaped fission yeast Schizosaccharomyces pombe cells, active GTP-bound Cdc42 promotes polarized growth at cell poles, while inactive Cdc42-GDP localizes ubiquitously also along cell sides. Zones of Cdc42 activity are maintained by positive feedback amplification involving the formation of a complex between Cdc42-GTP, the scaffold Scd2, and the guanine nucleotide exchange factor (GEF) Scd1, which promotes the activation of more Cdc42. Here, we use the CRY2-CIB1 optogenetic system to recruit and cluster a cytosolic Cdc42 variant at the plasma membrane and show that this leads to its moderate activation also on cell sides. Surprisingly, Scd2, which binds Cdc42-GTP, is still recruited to CRY2-Cdc42 clusters at cell sides in individual deletion of the GEFs Scd1 or Gef1. We show that activated Cdc42 clusters at cell sides are able to recruit Scd1, dependent on the scaffold Scd2. However, Cdc42 activity is not amplified by positive feedback and does not lead to morphogenetic changes, due to antagonistic activity of the GTPase activating protein Rga4. Thus, the cell architecture is robust to moderate activation of Cdc42 at cell sides.

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