Evidence map›Paper›PMID 27913677›Full record

ReviewBiochemical Society transactions2016

PHLPPing through history: a decade in the life of PHLPP phosphatases.

Agnieszka T Grzechnik, Alexandra C Newton

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

54 citing papers in PubMed, 85 citations in OpenAlex.

  1. PHLPP is neither a Phosphatase nor a Tumor Suppressor.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
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  14. PHLPP Signaling in Immune Cells.Current topics in microbiology and immunology · 2022
    Review
  15. Article
  16. Article
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  18. Review
  19. Myeloid Lineage Ablation ofInternational journal of molecular sciences · 2021
    Article
  20. Targeting Akt in cancer for precision therapy.Journal of hematology & oncology · 2021
    Review
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 1 institution in 1 country.

Agnieszka T GrzechnikBiomedical Sciences Graduate Program, University of California at San Diego, La Jolla, CA 92093-0721, U.S.A.
Alexandra C NewtonDepartment of Pharmacology, University of California at San Diego, La Jolla, CA 92093-0721, U.S.A.
University of California San Diego · US

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Signal Termination by PHLPP, PH domain Leucine-rich repeat Protein PhosphataseR01GM067946 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NEWTON, ALEXANDRA C. · 2003 to 2014
$4.1M
NIGMS NIH HHS R01 GM067946NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

In the decade since their discovery, the PH domain leucine-rich repeat protein phosphatases (PHLPP) have emerged as critical regulators of cellular homeostasis, and their dysregulation is associated with various pathophysiologies, ranging from cancer to degenerative diseases, such as diabetes and heart disease. The two PHLPP isozymes, PHLPP1 and PHLPP2, were identified in a search for phosphatases that dephosphorylate Akt, and thus suppress growth factor signaling. However, given that there are over 200 000 phosphorylated residues in a single cell, and fewer than 50 Ser/Thr protein phosphatases, it is not surprising that PHLPP has many other cellular functions yet to be discovered, including a recently identified role in regulating the epigenome. Both PHLPP1 and PHLPP2 are commonly deleted in human cancers, supporting a tumor suppressive role. Conversely, the levels of one isozyme, PHLPP1, are elevated in diabetes. Thus, mechanisms to correctly control PHLPP activity in cells are critical for normal cellular homeostasis. This review summarizes the known functions of PHLPP and its role in disease.

Indexed as

Signal TransductionAnimalsDiabetes MellitusGene Expression RegulationHumansNeoplasmsNuclear ProteinsPhosphoprotein PhosphatasesPhosphorylationProto-Oncogene Proteins c-aktNuclear ProteinsPHLPP1 protein, humanPHLPP2 protein, humanPhosphoprotein PhosphatasesProto-Oncogene Proteins c-aktPHLPP1PHLPP2phosphatasePP2Cprotein kinase Btumor suppressor

Identifiers

PMID27913677
PMCPMC5783572
OpenAlexW2559559781

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.