Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production

Ruediger, Ralf; Brewis, Neil; Ohst, Kim; Walter, Gernot

doi:10.1006/viro.1997.8873

Cited by 49HIV Research and TreatmentHIV/AIDS drug development and treatmentProtein Tyrosine Phosphatases

Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production

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Ruediger, Ralf, Brewis, Neil, Ohst, Kim, Walter, Gernot·1997·Virology

DOI 10.1006/viro.1997.8873

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Abstract

We demonstrated previously that PP2A exists in many cell types as two abundant forms: (1) holoenzyme composed of two regulatory subunits, A and B, and a catalytic subunit C; and (2) core enzyme consisting of the A and C subunits. These two forms have different substrate specificities. Since published data suggested that HIV-1 transcription may be regulated by a cellular protein phosphatase, it was of interest to determine whether changing the ratio between PP2A core and holoenzyme affects HIV-1 gene expression. This question was addressed by expression in COS cells of an N-terminal mutant of the A subunit, A delta 5, which binds the C but not the B subunit. This resulted in an increase in the amount of core enzyme and a decrease in the amount of holoenzyme concomitant with the expected change in phosphatase activity. Tat-stimulated transcription from the HIV-1 LTR was inhibited 5-fold by mutant A delta 5, whereas mRNA synthesis directed by the actin promoter was not affected. Furthermore, virus production in COS, HeLa, and Jurkat T cells was inhibited 45-, 5-, and 3-fold, respectively, by mutant A delta 5. These results demonstrate that the balance between PP2A holoenzyme and core enzyme is important for HIV-1 gene expression and virus production.

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The AΔ5 mutant cannot bind any B subunit class and would therefore act as a dominant-negative mutant toward several different PP2A trimers.
“The AΔ5 mutant is incapable of binding any B subunit class [66] and would therefore behave as a dominantnegative mutant towards several different PP2A trimers.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [66]
The Aα Δ5 variant, found in human breast carcinoma and lacking HEAT-repeat 5, no longer binds any B subunit.
“The Aα Δ5 variant, found in human breast carcinoma [104] and lacking HEAT-repeat 5, no longer bound any B subunit [66].”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [66]

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Self-citation

α4 Is an Essential Regulator of PP2A Phosphatase Activity
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Pertussis Toxin Modification of PC12 Cells Inhibits a Protein Phosphatase 2A‐Like Phosphatase
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Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases.Preprint
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Authors: Ruediger, R., Brewis, N., Ohst, K., & Walter, G.
Affiliations: University of California San Diego (US)
Corresponding author: Walter, Gernot
ORCID: Brewis, Neil
Venue: Virology
Publisher: Elsevier BV
Published: 1997-11
Volume: 238
Issue: 2
Pages: 432-443
ISSN: 0042-6822 (ISSN-L)
DOI: 10.1006/viro.1997.8873
OpenAlex: W2039509022
Cited by: 49
References: 78
Citations by year: 2026: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2014: 1 · 2013: 2 · 2012: 1
FWCI: 0.81
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5737 d)
Locations: Virology (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Veterans Affairs
National Institutes of Health (AI-38858, AI 27670)
Center for AIDS Research, University of Washington
University of California, San Diego (AI 36214)
National Institute of Allergy and Infectious Diseases (AI38858, AI-36214, U01AI038858, U01AI027670, AI2-7670, P30AI036214)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: protein phosphatase 2A, holoenzyme, core enzyme, HIV-1 transcription, HIV-1 LTR, Tat, HIV-1 gene expression, virus production, substrate specificity
MeSH terms: Animals, Coenzymes, HeLa Cells, Humans, Mutation, Phosphoprotein Phosphatases, Promoter Regions, Genetic, RNA, Messenger, Transcription, Genetic, HIV-1, Gene Products, tat, Gene Expression Regulation, Viral, HIV Long Terminal Repeat, Jurkat Cells, COS Cells, tat Gene Products, Human Immunodeficiency Virus

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Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production

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