Yeast Protein Serine/Threonine Phosphatases: Multiple Roles and Diverse Regulation

Stark, Michael J. R.

doi:10.1002/(sici)1097-0061(199612)12:16<1647::aid-yea71>3.0.co;2-q

Cited by 186 publications

(123 citation statements)

References 192 publications

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“…For instance, Sac. cerevisiae has approximately 6000 genes, of which 113 encode protein kinase genes, but only 31 encode protein phosphatases (Dickman & Yarden, 1999;Sakumoto et al, 1999;Stark, 1996). Considering the deviation in prevalence between protein kinases and protein phosphatases, it is likely that Cpp1 has broad substrate specificity, and interacts with multiple protein kinases in several signalling pathways.…”

Section: Discussionmentioning

confidence: 99%

“…Considering the deviation in prevalence between protein kinases and protein phosphatases, it is likely that Cpp1 has broad substrate specificity, and interacts with multiple protein kinases in several signalling pathways. Further complicating the process, a 36 kDa PP2A catalytic subunit combines with a 65 kDa regulatory subunit to form a PP2A holoenzyme dimer, with a third variable subunit, known as the B subunit, responsible for substrate specificity (Stark, 1996;Mayer-Jaekel & Hemmings, 1994). Since CPP1 encodes a putative catalytic subunit of PP2A, the broad specificity of substrates of CPP1 may be narrowed with additional protein phosphatase subunit components (Mayer-Jaekel & Hemmings, 1994).…”

Section: Discussionmentioning

confidence: 99%

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Functional characterization of Fusarium verticillioides CPP1, a gene encoding a putative protein phosphatase 2A catalytic subunit

Choi

Shim

2008

Microbiology

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Fusarium verticillioides produces the mycotoxin fumonisin B 1 (FB 1 ) on maize kernels. In this study, we identified a putative protein phosphatase gene CPP1 in F. verticillioides, and investigated its role in FB 1 regulation. Previous work has shown that CPP1 expression is elevated in an FB 1 -suppressing genetic background. Thus, we hypothesized that CPP1 is negatively associated with FB 1 production. To test this hypothesis, we generated a CPP1 knockout mutant, PP179, and studied the effects of gene deletion on FB 1 biosynthesis and fungal development. PP179 showed elevated expression of FUM genes, and in turn produced higher levels of FB 1 than the wild-type progenitor. Other significant mutant phenotypes included reduced radial growth on agar plates, reduced conidia germination rates, significantly increased macroconidia formation, and hyphal swelling. To verify that these phenotypes were directly due to CPP1 deletion, we complemented PP179 with the wild-type CPP1 gene. The complemented strain PPC4 showed FUM1 expression and FB 1 production similar to that of the wild-type, providing evidence that CPP1 is negatively associated with FB 1 biosynthesis. Other PP179 phenotypes, such as macroconidiation and hyphal swelling, were also restored to that of wild-type progenitor. Furthermore, we complemented F. verticillioides PP179 strain with Neurospora crassa wild-type ppe-1 gene, demonstrating that Cpp1 and PPE-1 proteins are functionally conserved. Pleiotropic effects of CPP1 deletion led us to hypothesize that CPP1 is associated with multiple downstream signalling pathways in F. verticillioides. Identification and functional characterization of downstream Cpp1-interacting proteins are necessary to better understand the complex regulatory mechanisms associated with Cpp1.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Functional characterization of Fusarium verticillioides CPP1, a gene encoding a putative protein phosphatase 2A catalytic subunit

Choi

Shim

2008

Microbiology

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“…The fact that loss of PP1 function in other organisms also causes mitotic arrest suggests that the role of PP1 and, thus, the consequences of its deficiency, might be highly conserved. Precedence for the conservation of PP1 function is found in glycogen metabolism where PP1 holoenzymes, composed of the PP1 catalytic subunit and a glycogen-targeting subunit, is thought to dephosphorylate glycogen synthase in both yeast (Stark 1996) and mammals (Hubbard and Cohen 1993). The specificity of PP1 is thought to be regulated by subunits that target PP1 to its substrate and/or regulate its activity (Hubbard and Cohen 1993).…”

Section: Discussionmentioning

confidence: 99%

“…Four other cells had not undergone cytokinesis at the completion of the time-lapse data acquisition (>54, 92, 116, and 124 min after mid-anaphase). Interestingly, a defect or delay in cytokinesis is caused by another allele of GLC7 (Stark 1996).…”

Section: Glc7-129 Cells Delay In G 2 /M With a Short Spindlementioning

confidence: 99%

Defects in Saccharomyces cerevisiae protein phosphatase type I activate the spindle/kinetochore checkpoint

Bloecher

Tatchell²

1999

Genes & Development

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“…Glc7p is an essential type 1 protein phosphatase localized in the nucleus and the cytosol, and known to participate in diverse cellular processes (Stark, 1996). Although it has recently been implicated in the regulation of actin organization and endocytosis by the finding that it interacts with Scd5p , its exact function in this aspect has remained unexplored.…”

Section: Glc7p As the Phosphatase For Pan1p Dephosphorylationmentioning

confidence: 99%

Scd5p Mediates Phosphoregulation of Actin and Endocytosis by the Type 1 Phosphatase Glc7p in Yeast

Zeng

Neo

Wang

et al. 2007

MBoC

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Pan1p plays essential roles in both actin and endocytosis in yeast. It interacts with, and regulates the function of, multiple endocytic proteins and actin assembly machinery. Phosphorylation of Pan1p by the kinase Prk1p down-regulates its activity, resulting in disassembly of the endocytic vesicle coat complex and termination of vesicle-associated actin polymerization. In this study, we focus on the mechanism that acts to release Pan1p from phosphorylation inhibition. We show that Pan1p is dephosphorylated by the phosphatase Glc7p, and the dephosphorylation is dependent on the Glc7p-targeting protein Scd5p, which itself is a phosphorylation target of Prk1p. Scd5p links Glc7p to Pan1p in two ways: directly by interacting with Pan1p and indirectly by interacting with the Pan1p-binding protein End3p. Depletion of Glc7p from the cells causes defects in cell growth, actin organization, and endocytosis, all of which can be partially suppressed by deletion of the PRK1 gene. These results suggest that Glc7p antagonizes the activity of the Prk1p kinase in regulating the functions of Pan1p and possibly other actin-and endocytosis-related proteins.

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Yeast Protein Serine/Threonine Phosphatases: Multiple Roles and Diverse Regulation

Cited by 186 publications

References 192 publications

Functional characterization of Fusarium verticillioides CPP1, a gene encoding a putative protein phosphatase 2A catalytic subunit

Functional characterization of Fusarium verticillioides CPP1, a gene encoding a putative protein phosphatase 2A catalytic subunit

Defects in Saccharomyces cerevisiae protein phosphatase type I activate the spindle/kinetochore checkpoint

Scd5p Mediates Phosphoregulation of Actin and Endocytosis by the Type 1 Phosphatase Glc7p in Yeast

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