CoChat
Sign Up
Cited by 38Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingAlzheimer's disease research and treatments

Altered phosphorylation of cytoskeletal proteins in mutant protein phosphatase 2A transgenic mice

Schild, Andreas, Ittner, Lars M., Götz, Jürgen·2006·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2006.03.066
Open this paper in CoChat — free account

Abstract

Protein phosphatase 2A (PP2A) is a family of heterotrimeric enzymes with diverse functions under physiologic and pathologic conditions such as Alzheimer's disease. All PP2A holoenzymes have in common a catalytic subunit C and a structural scaffolding subunit A. These core subunits assemble with various regulatory B subunits to form heterotrimers with distinct functions in the cell. Substrate specificity of PP2A in vitro is determined by regulatory subunits with leucine 309 of the catalytic subunit C playing a crucial role in the recruitment of regulatory subunits into the complex. Here we expressed a mutant form of Calpha, L309A, in brain and Harderian (lacrimal) gland of transgenic mice. We found an altered recruitment of regulatory subunits into the complex, demonstrating a role for the carboxyterminal leucine of Calpha in regulating holoenzyme assembly in vivo. This was associated with an increased phosphorylation of tau in brain and an impaired dephosphorylation of vimentin demonstrating that both cytoskeletal proteins are in vivo substrates of distinct PP2A holoenzyme complexes.

Integrity signals

Registry

Crossref · 10.1016/j.bbrc.2006.03.066

Cites

61 of 61 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • In vivo neuron-specific expression of a Cα mutant with the L309A substitution (which prevents B55 subunit binding) resulted in increased tau phosphorylation (Ser202/Thr205) and impaired dephosphorylation of vimentin, but no neurodegeneration.

    “In vivo neuron-specific expression of a Cα mutant, harboring the L309A substitution in the C-terminal tail that does not affect PP2A-C methylation but specifically prevents B55 subunit binding [40], resulted in increased tau phosphorylation (Ser202/Thr205) and impaired dephosphorylation of vimentin, but no neurodegeneration [49].”

    From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [49]

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Related

Authors
Schild, A., Ittner, L. M., & Götz, J.
Affiliations
  • University of Zurich (CH)
  • The University of Sydney (AU)
Corresponding author
Götz, Jürgen
ORCID
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2006-05
Volume
343
Issue
4
Pages
1171-1178
ISSN
0006-291X (ISSN-L)
DOI
10.1016/j.bbrc.2006.03.066
OpenAlex
W2051641212
Cited by
38
References
61
Citations by year
2025: 2 · 2022: 1 · 2021: 2 · 2020: 2 · 2018: 1 · 2017: 3 · 2014: 2 · 2013: 3 · 2012: 2
FWCI
1.76
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
  • Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
Funders
  • University of Sydney
  • Medical Foundation
  • Austrian Science Fund (P15685)
  • nccr – on the move
  • EMDO Stiftung
  • Kurt und Senta Herrmann Stiftung
  • Olga Mayenfisch Stiftung
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
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
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Keywords
protein phosphatase 2A, holoenzyme assembly, tau phosphorylation, transgenic mice, Harderian gland, Alzheimer's disease
MeSH terms
Animals, Brain, Cytoskeleton, Harderian Gland, Leucine, Mice, Transgenic, Mutation, Phosphoprotein Phosphatases, Phosphorylation, Vimentin, tau Proteins, Protein Subunits, Mice, Protein Phosphatase 2

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review