Evidence map›Paper›PMID 22815089›Full record

ReviewIUBMB life2012

Endogenous inhibitor proteins that connect Ser/Thr kinases and phosphatases in cell signaling.

Masumi Eto, David L Brautigan

Abstract readReview
In one paragraph

Review in IUBMB life, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.5field-weighted citation impact, top 35% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
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  8. Possible roles of N- and C-terminal unstructured tails of CPI-17 in regulating CaJournal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2022
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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 at 2 institutions in 1 country.

Masumi EtoDepartment of Molecular Physiology and Biophysics, and Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107, USA. masumi.eto@jefferson.edu
David L Brautigan
Jefferson Institute · USUniversity of Virginia · US

Funding

Phosphorylation & Function of Inhibitor-2R01GM056362 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI BRAUTIGAN, DAVID L. · 1997 to 2011
$2.4M
IR signaling through PP6, a potential molecular target for radiosensitizationR01CA142823 · NCI · UNIVERSITY OF VIRGINIA · PI LARNER, JAMES M · 2010 to 2014
$1.5M
Regulation Vascular Smooth Muscle Myosin PhosphataseR01HL083261 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI ETO, MASUMI · 2006 to 2010
$1.3M
Myosin phosphatase autoinhibition in gastrointestinal smooth muscle contractionR01DK088905 · NIDDK · UNIVERSITY OF VIRGINIA · PI ETO, MASUMI, SOMLYO, AVRIL V. · 2010 to 2012
$1.1M
NCI NIH HHS CA142823NCI NIH HHS R01 CA142823NHLBI NIH HHS R01 HL083261NHLBI NIH HHS R01HL083261NIDDK NIH HHS R01 DK088905NIDDK NIH HHS R01DK088905NIGMS NIH HHS R01 GM056362NIGMS NIH HHS R01 GM56362
6 · The paper itself

Abstract

Protein phosphatase activity acts as a primary determinant of the extent and duration of phosphorylation of cellular proteins in response to physiological stimuli. Ser/Thr protein phosphatase-1 (PP1) belongs to the PPP superfamily, and is associated with regulatory subunits that confer substrate specificity, allosteric regulation, and subcellular compartmentalization. In addition, all eukaryotic cells contain multiple heat-stable proteins that originally were thought to inhibit phosphatase catalytic subunits released from the regulatory subunits, as a fail-safe mechanism. However, discovery of C-kinase-activated PP1 inhibitor, Mr of 17 kDa (CPI-17) required fresh thinking about the endogenous inhibitors as specific regulators of particular phosphatase complexes, acting in addition to, not instead of, regulatory subunits. The cellular actions of the endogenous inhibitors are controlled by phosphorylation, connecting them to kinase pathways. More recent progress has unveiled additional functions of PP1 inhibitor-2 (I-2), including regulation of protein kinases. Transcriptional mechanisms govern the expression levels of CPI-17 in response to stimuli. If true for other inhibitor proteins, they have the potential of being diagnostic markers for pathological conditions. We discuss specific examples of PP1 inhibitor proteins regulating particular cellular functions and the rationale for incorporating phosphatase inhibitor proteins in development of new therapeutic strategies.

Indexed as

Signal TransductionAnimalsGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsPhosphoprotein PhosphatasesProtein BindingProtein Interaction Domains and MotifsProtein Serine-Threonine KinasesIntracellular Signaling Peptides and ProteinsPhosphoprotein PhosphatasesProtein Serine-Threonine Kinases

Identifiers

PMID22815089
PMCPMC3422418
OpenAlexW2016479254

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.