Evidence map›Paper›PMID 11336659›Full record

ArticleThe Biochemical journal2001

Cloning and identification of MYPT3: a prenylatable myosin targetting subunit of protein phosphatase 1.

J A Skinner, A R Saltiel

Abstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

  1. Article
  2. LMTK2 switches on canonical TGF-β1 signaling in human bronchial epithelial cells.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. TIMAP is a positive regulator of pulmonary endothelial barrier function.American journal of physiology. Lung cellular and molecular physiology · 2008
    Article
  11. Epistasis between hyperglycemic QTLs revealed in a double congenic of the OLETF rat.Mammalian genome : official journal of the International Mammalian Genome Society · 2007
    Article
  12. Article
  13. Signal transduction therapeutics: relevance for Alzheimer's disease.Journal of molecular neuroscience : MN · 2004
    Review
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

J A SkinnerDepartment of Cell Biology, Pfizer Global Research and Development, Ann Arbor Laboratories, 2800 Plymouth Road, Ann Arbor, MI 48105, USA.
A R Saltiel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To identify novel protein phosphatase 1 (PP1)-interacting proteins, a yeast two-hybrid 3T3-L1 adipocyte cDNA library was screened with the catalytic subunit of PP1 as bait. In the present work, the isolation, identification and initial biochemical characterization of a novel PP1-interacting protein, MYPT3, which is homologous with the myosin phosphatase targetting subunit (MYPT) family, is described. MYPT3 aligns >99% with a region of mouse genomic DNA clone RP23-156P23 and localizes to chromosome 15, between markers at 44.1-46.5 cM, as demonstrated by radiation hybrid mapping. The gene consists of ten exons that encode for a 524-amino acid sequence with a predicted molecular mass of 57529 Da. The N-terminal region of MYPT3 consists of a consensus PP1-binding site and multiple ankyrin repeats. MYPT3 is distinguished from related approximately 110-130 kDa MYPT subunits by its molecular mass of 58 kDa, and a unique C-terminal region that contains several potential signalling motifs and a CaaX prenylation site. We have shown that affinity-purified glutathione S-transferase (GST)-MYPT3 is prenylated by purified recombinant farnesyltransferase in vitro. Endogenous PP1 from 3T3-L1 lysates specifically interacts with MYPT3. Additionally, purified PP1 activity was inhibited by GST-MYPT3 toward phosphorylase a, myosin light chain and myosin substrate in vitro. Overall, our findings identify a novel prenylatable subunit of PP1 that defines a new subfamily of MYPT.

Indexed as

Protein PrenylationProtein Sorting Signals3T3 CellsAmino Acid SequenceAnimalsChromosome MappingCloning, MolecularMiceMolecular Sequence DataMyosin Light ChainsMyosinsPhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Phosphatase 1Protein SubunitsMyosin Light ChainsMyosinsPhosphoprotein PhosphatasesProtein Phosphatase 1Protein Sorting SignalsProtein Subunits

Identifiers

PMID11336659
PMCPMC1221835

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.