Evidence map›Paper›PMID 34353431›Full record

ReviewBMB reports2021

Emerging roles of PHLPP phosphatases in metabolism.

Jong-Ho Cha, Yelin Jeong, Ah-Reum Oh, Sang Bae Lee, Soon-Sun Hong, KyeongJin Kim

Open access · goldAbstract readReview
In one paragraph

Review in BMB reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

9 citing papers in PubMed, 10 citations in OpenAlex.

  1. PHLPP is neither a Phosphatase nor a Tumor Suppressor.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
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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

6 authors at 2 institutions in 1 country.

Jong-Ho ChaDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212; Program in Biomedical Science & Engineering, Inha University, Incheon 22212, Korea.
Yelin JeongDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212; Program in Biomedical Science & Engineering, Inha University, Incheon 22212; Research Center for Controlling Intercellular Communication (RCIC), College of Medicine, Inha University, Incheon 22212, Korea.
Ah-Reum OhDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212; Program in Biomedical Science & Engineering, Inha University, Incheon 22212; Research Center for Controlling Intercellular Communication (RCIC), College of Medicine, Inha University, Incheon 22212, Korea.
Sang Bae LeeDivision of Life Sciences, Jeonbuk National University; Sarcopenia Total Solution Center, Jeonju 54896, Korea.
Soon-Sun HongDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212; Program in Biomedical Science & Engineering, Inha University, Incheon 22212; Research Center for Controlling Intercellular Communication (RCIC), College of Medicine, Inha University, Incheon 22212, Korea.
KyeongJin KimDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212; Program in Biomedical Science & Engineering, Inha University, Incheon 22212; Research Center for Controlling Intercellular Communication (RCIC), College of Medicine, Inha University, Incheon 22212, Korea.
Inha University · KRJeonbuk National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over the last decades, research has focused on the role of pleckstrin homology (PH) domain leucine-rich repeat protein phosphatases (PHLPPs) in regulating cellular signaling via PI3K/Akt inhibition. The PKB/Akt signaling imbalances are associated with a variety of illnesses, including various types of cancer, inflammatory response, insulin resistance, and diabetes, demonstrating the relevance of PHLPPs in the prevention of diseases. Furthermore, identification of novel substrates of PHLPPs unveils their role as a critical mediator in various cellular processes. Recently, researchers have explored the increasing complexity of signaling networks involving PHLPPs whereby relevant information of PHLPPs in metabolic diseases was obtained. In this review, we discuss the current knowledge of PHLPPs on the well-known substrates and metabolic regulation, especially in liver, pancreatic beta cell, adipose tissue, and skeletal muscle in relation with the stated diseases. Understanding the context-dependent functions of PHLPPs can lead to a promising treatment strategy for several kinds of metabolic diseases. [BMB Reports 2021; 54(9): 451-457].

Indexed as

Adipose TissueHumansInsulin ResistanceLiverMetabolic DiseasesPhosphatidylinositol 3-KinasesPhosphoprotein PhosphatasesProto-Oncogene Proteins c-aktSignal TransductionSubstrate SpecificityPhosphatidylinositol 3-KinasesPhosphoprotein PhosphatasesProto-Oncogene Proteins c-akt

Identifiers

PMID34353431
PMCPMC8505235
OpenAlexW3192803448

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.