scholarly journals Structure and dimerization of the catalytic domain of the protein phosphatase Cdc14p, a key regulator of mitotic exit in Saccharomyces cerevisiae

2017 ◽  
Vol 26 (10) ◽  
pp. 2105-2112 ◽  
Author(s):  
Junya Kobayashi ◽  
Yoshiyuki Matsuura
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Phosphatase ◽  
Catalytic Domain ◽  
Mitotic Exit

scholarly journals Protein Phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae

2020 ◽  
Author(s):  
Dilara Kocakaplan ◽  
Hüseyin Karabürk ◽  
Cansu Dilege ◽  
Idil Kirdok ◽  
Şeyma Nur Erkan ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mitotic Spindle ◽  
Protein Phosphatase ◽  
Budding Yeast ◽  
Mitotic Exit ◽  
Protein Phosphatase 1 ◽  
Inhibitory Function ◽  
Surveillance Mechanism ◽  
Spindle Position

AbstractSaccharomyces cerevisiae, also known as the budding yeast, orients and elongates its mitotic spindle along its polarity axis in order to segregate one copy of its genomic DNA to the daughter cell. When accurate positioning of the mitotic spindle fails, a surveillance mechanism, named the Spindle Position Checkpoint (SPOC), prevents cells from exiting mitosis unless the spindle orientation is corrected. Mutants with a defective SPOC loss their genomic integrity, become multiploid and aneuploid. Thus, SPOC is a crucial checkpoint for the budding yeast. Yet, a comprehensive understanding of how the SPOC mechanism works is missing. In this study, we identified Bud14 as a novel checkpoint protein. We showed that the mitotic exit inhibitory function of Bud14 requires its association with the type 1 protein phosphatase, Glc7. Our data indicate that Glc7-Bud14 promotes dephosphorylation of the SPOC effector protein Bfa1. Our results support a model in which Glc7-Bud14 works parallel to the SPOC kinase Kin4 in inhibiting mitotic exit.

scholarly journals The N-Terminal Region of Yeast Protein Phosphatase Ppz1 Is a Determinant for Its Toxicity

2020 ◽  
Vol 21 (20) ◽  
pp. 7733
Author(s):  
Carlos Calafí ◽  
María López-Malo ◽  
Marcel Albacar ◽  
Antonio Casamayor ◽  
Joaquín Ariño
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Proliferation ◽  
Protein Phosphatase ◽  
Catalytic Domain ◽  
Cell Periphery ◽  
Hybrid Protein ◽  
Yeast Protein ◽  
Toxic Protein ◽  
Intrinsically Disordered ◽  
Intermediate Effect

The Ppz enzymes are Ser/Thr protein phosphatases present only in fungi that are characterized by a highly conserved C-terminal catalytic region, related to PP1c phosphatases, and a more divergent N-terminal extension. In Saccharomyces cerevisiae, Ppz phosphatases are encoded by two paralog genes, PPZ1 and PPZ2. Ppz1 is the most toxic protein when overexpressed in budding yeast, halting cell proliferation, and this effect requires its phosphatase activity. We show here that, in spite of their conserved catalytic domain, Ppz2 was not toxic when tested under the same conditions as Ppz1, albeit Ppz2 levels were somewhat lower. Remarkably, a hybrid protein composed of the N-terminal extension of Ppz1 and the catalytic domain of Ppz2 was as toxic as Ppz1, even if its expression level was comparable to that of Ppz2. Similar amounts of yeast PP1c (Glc7) produced an intermediate effect on growth. Mutation of the Ppz1 myristoylable Gly2 to Ala avoided the localization of the phosphatase at the cell periphery but only slightly attenuated its toxicity. Therefore, the N-terminal extension of Ppz1 plays a key role in defining Ppz1 toxicity. This region is predicted to be intrinsically disordered and contains several putative folding-upon-binding regions which are absent in Ppz2 and might be relevant for toxicity.

scholarly journals Dbf2–Mob1 drives relocalization of protein phosphatase Cdc14 to the cytoplasm during exit from mitosis

2009 ◽  
Vol 184 (4) ◽  
pp. 527-539 ◽  
Author(s):  
Dane A. Mohl ◽  
Michael J. Huddleston ◽  
Therese S. Collingwood ◽  
Roland S. Annan ◽  
Raymond J. Deshaies
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Localization ◽  
Protein Phosphatase ◽  
Nuclear Localization Signal ◽  
Mitotic Exit ◽  
Cyclin Dependent Kinase ◽  
Mitotic Exit Network ◽  
Localization Signal ◽  
Precipitous Decline ◽  
Component Protein

Exit from mitosis is characterized by a precipitous decline in cyclin-dependent kinase (Cdk) activity, dissolution of mitotic structures, and cytokinesis. In Saccharomyces cerevisiae, mitotic exit is driven by a protein phosphatase, Cdc14, which is in part responsible for counteracting Cdk activity. Throughout interphase, Cdc14 is sequestered in the nucleolus, but successful anaphase activates the mitotic exit network (MEN), which triggers dispersal of Cdc14 throughout the cell by a mechanism that has remained unknown. In this study, we show that a MEN component, protein kinase Dbf2–Mob1, promotes transfer of Cdc14 to the cytoplasm and consequent exit from mitosis by direct phosphorylation of Cdc14 on serine and threonine residues adjacent to a nuclear localization signal (NLS), thereby abrogating its NLS activity. Our results define a mechanism by which the MEN promotes exit from mitosis.

scholarly journals The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae.

1994 ◽  
Vol 269 (12) ◽  
pp. 8792-8796
Author(s):  
I. Mendoza ◽  
F. Rubio ◽  
A. Rodriguez-Navarro ◽  
J.M. Pardo
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Phosphatase ◽  
Nacl Tolerance

CDC55, a Saccharomyces cerevisiae gene involved in cellular morphogenesis: identification, characterization, and homology to the B subunit of mammalian type 2A protein phosphatase

1991 ◽  
Vol 11 (11) ◽  
pp. 5767-5780
Author(s):  
A M Healy ◽  
S Zolnierowicz ◽  
A E Stapleton ◽  
M Goebl ◽  
A A DePaoli-Roach ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Phosphatase ◽  
Protein A ◽  
Cdna Clones ◽  
Restrictive Temperature ◽  
B Subunit ◽  
Bud Emergence ◽  
New Gene ◽  
Cold Sensitive ◽  
Polymerase Chain

Microscopic screening of a collection of cold-sensitive mutants of Saccharomyces cerevisiae led to the identification of a new gene, CDC55, which appears to be involved in the morphogenetic events of the cell cycle. CDC55 maps between CDC43 and CHC1 on the left arm of chromosome VII. At restrictive temperature, the original cdc55 mutant produces abnormally elongated buds and displays a delay or partial block of septation and/or cell separation. A cdc55 deletion mutant displays a cold-sensitive phenotype like that of the original isolate. Sequencing of CDC55 revealed that it encodes a protein of about 60 kDa, as confirmed by Western immunoblots using Cdc55p-specific antibodies. This protein has greater than 50% sequence identity to the B subunits of rabbit skeletal muscle type 2A protein phosphatase; the latter sequences were obtained by analysis of peptides derived from the purified protein, a polymerase chain reaction product, and cDNA clones. An extragenic suppressor of the cdc55 mutation lies in BEM2, a gene previously identified on the basis of an apparent role in bud emergence.

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