Cited by 42Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingFungal and yeast genetics research

Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2

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Van HOOF, Christine, MARTENS, Ellen, LONGIN, Sari, JORDENS, Jan, STEVENS, Ilse, JANSSENS, Veerle, GORIS, Jozef·2005·Biochemical Journal

Abstract

To elucidate the specific biological role of the yeast homologues of PTPA (phosphatase 2A phosphatase activator), Ypa1 and Ypa2 (where Ypa stands for yeast phosphatase activator), in the regulation of PP2A (protein phosphatase 2A), we investigated the physical interaction of both Ypa proteins with the catalytic subunit of the different yeast PP2A-like phosphatases. Ypa1 interacts specifically with Pph3, Sit4 and Ppg1, whereas Ypa2 binds to Pph21 and Pph22. The Ypa1 and Ypa2 proteins do not compete with Tap42 (PP2A associating protein) for binding to PP2A family members. The interaction of the Ypa proteins with the catalytic subunit of PP2A-like phosphatases is direct and independent of other regulatory subunits, implicating a specific function for the different PP2A-Ypa complexes. Strikingly, the interaction of Ypa2 with yeast PP2A is promoted by the presence of Ypa1, suggesting a positive role of Ypa1 in the regulation of PP2A association with other interacting proteins. As in the mammalian system, all yeast PP2A-like enzymes associate as an inactive complex with Yme (yeast methyl esterase). Ypa1 as well as Ypa2 can reactivate all these inactive complexes, except Pph22-Yme. Ypa1 is the most potent activator of PP2A activity, suggesting that there is no direct correlation between activation potential and binding capacity.

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  • Caution is needed when interpreting biogenesis regulator strains because several of these proteins also affect PP4 and PP6, so their knockout or overexpression may not affect only PP2A.

    “Some caution in interpreting data for the PP2A biogenesis regulator strains is however warranted, as several of these proteins, besides PP2A, likely also affect the functions of the PP2A-like phosphatases PP4 and PP6 [23][24][25][26], and hence, their knockout or overexpression may not solely affect PP2A.”

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Authors
Van HOOF, C., MARTENS, E., LONGIN, S., JORDENS, J., STEVENS, I., JANSSENS, V., & GORIS, J.
Affiliations
  • Afdeling Biochemie, Faculteit Geneeskunde, Campus Gasthuisberg O&N, Katholieke Universiteit Leuven, Herestraat 49, B-3000 Leuven, Belgium
  • KU Leuven (BE)
Venue
Biochemical Journal
Published
2005-02-08
Volume
386
Issue
1
Pages
93-102
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W2032966848
Cited by
42
References
32
Citations by year
2023: 1 · 2020: 1 · 2019: 1 · 2018: 3 · 2017: 2 · 2015: 2 · 2014: 4 · 2013: 3 · 2012: 6
FWCI
1.64
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Lirias (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
protein phosphatase 2A, PTPA, protein-protein interaction, triphenylphosphine, Sit4, phosphatase activation, protein phosphatase regulation, Saccharomyces cerevisiae
MeSH terms
Carboxylic Ester Hydrolases, Enzyme Activation, Phosphoprotein Phosphatases, Phosphorylation, Protein Binding, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Structure-Activity Relationship, Peptidylprolyl Isomerase, Sirolimus, Catalytic Domain, Two-Hybrid System Techniques, Protein Subunits, Protein Interaction Mapping, Saccharomyces cerevisiae Proteins, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Protein Phosphatase 2

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