Symmetric dimethylation on histone H4R3 associates with histone deacetylation to maintain properly polarized cell growth

2020 ◽  
Vol 171 (2) ◽  
pp. 91-98
Author(s):  
Ruxin Duan ◽  
Hong-Yeoul Ryu ◽  
Seong Hoon Ahn
2018 ◽  
Vol 28 (7) ◽  
pp. 1039-1051.e5 ◽  
Author(s):  
Nika Pende ◽  
Jinglan Wang ◽  
Philipp M. Weber ◽  
Jolanda Verheul ◽  
Erkin Kuru ◽  
...  

2004 ◽  
Vol 164 (2) ◽  
pp. 207-218 ◽  
Author(s):  
Scott Bidlingmaier ◽  
Michael Snyder

The dynamic regulation of polarized cell growth allows cells to form structures of defined size and shape. We have studied the regulation of polarized growth using mating yeast as a model. Haploid yeast cells treated with high concentration of pheromone form successive mating projections that initiate and terminate growth with regular periodicity. The mechanisms that control the frequency of growth initiation and termination under these conditions are not well understood. We found that the polarisome components Spa2, Pea2, and Bni1 and the Cdc42 regulators Cdc24 and Bem3 control the timing and frequency of projection formation. Loss of polarisome components and mutation of Cdc24 decrease the frequency of projection formation, while loss of Bem3 increases the frequency of projection formation. We found that polarisome components and the cell fusion proteins Fus1 and Fus2 are important for the termination of projection growth. Our results define the first molecular regulators that control the timing of growth initiation and termination during eukaryotic cell differentiation.


PLoS Genetics ◽  
2012 ◽  
Vol 8 (10) ◽  
pp. e1003004 ◽  
Author(s):  
K. Adam Bohnert ◽  
Kathleen L. Gould

2016 ◽  
Vol 212 (1) ◽  
pp. 51-61 ◽  
Author(s):  
Erin M. Jonasson ◽  
Valentina Rossio ◽  
Riko Hatakeyama ◽  
Mitsuhiro Abe ◽  
Yoshikazu Ohya ◽  
...  

Budding yeast Rho1 guanosine triphosphatase (GTPase) plays an essential role in polarized cell growth by regulating cell wall glucan synthesis and actin organization. Upon cell wall damage, Rho1 blocks polarized cell growth and repairs the wounds by activating the cell wall integrity (CWI) Pkc1–mitogen-activated protein kinase (MAPK) pathway. A fundamental question is how active Rho1 promotes distinct signaling outputs under different conditions. Here we identified the Zds1/Zds2–protein phosphatase 2ACdc55 (PP2ACdc55) complex as a novel Rho1 effector that regulates Rho1 signaling specificity. Zds1/Zds2–PP2ACdc55 promotes polarized growth and cell wall synthesis by inhibiting Rho1 GTPase-activating protein (GAP) Lrg1 but inhibits CWI pathway by stabilizing another Rho1 GAP, Sac7, suggesting that active Rho1 is biased toward cell growth over stress response. Conversely, upon cell wall damage, Pkc1–Mpk1 activity inhibits cortical PP2ACdc55, ensuring that Rho1 preferentially activates the CWI pathway for cell wall repair. We propose that PP2ACdc55 specifies Rho1 signaling output and that reciprocal antagonism between Rho1–PP2ACdc55 and Rho1–Pkc1 explains how only one signaling pathway is robustly activated at a time.


Genetics ◽  
2014 ◽  
Vol 197 (4) ◽  
pp. 1191-1200 ◽  
Author(s):  
Tianlu Li ◽  
Borja Belda-Palazón ◽  
Alejandro Ferrando ◽  
Paula Alepuz

1994 ◽  
Vol 127 (5) ◽  
pp. 1381-1394 ◽  
Author(s):  
Y J Kim ◽  
L Francisco ◽  
G C Chen ◽  
E Marcotte ◽  
C S Chan

The IPL2 gene is known to be required for normal polarized cell growth in the budding yeast Saccharomyces cerevisiae. We now show that IPL2 is identical to the previously identified BEM2 gene. bem2 mutants are defective in bud site selection at 26 degrees C and localized cell surface growth and organization of the actin cytoskeleton at 37 degrees C. BEM2 encodes a protein with a COOH-terminal domain homologous to sequences found in several GTPase-activating proteins, including human Bcr. The GTPase-activating protein-domain from the Bem2 protein (Bem2p) or human Bcr can functionally substitute for Bem2p. The Rho1 and Rho2 GTPases are the likely in vivo targets of Bem2p because bem2 mutant phenotypes can be partially suppressed by increasing the gene dosage of RHO1 or RHO2. CDC55 encodes the putative regulatory B subunit of protein phosphatase 2A, and mutations in BEM2 have previously been identified as suppressors of the cdc55-1 mutation. We show here that mutations in the previously identified GRR1 gene can suppress bem2 mutations. grr1 and cdc55 mutants are both elongated in shape and cold-sensitive for growth, and cells lacking both GRR1 and CDC55 exhibit a synthetic lethal phenotype. bem2 mutant phenotypes also can be suppressed by the SSD1-vl (also known as SRK1) mutation, which was shown previously to suppress mutations in the protein phosphatase-encoding SIT4 gene. Cells lacking both BEM2 and SIT4 exhibit a synthetic lethal phenotype even in the presence of the SSD1-v1 suppressor. These genetic interactions together suggest that protein phosphorylation and dephosphorylation play an important role in the BEM2-mediated process of polarized cell growth.


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