Evidence map›Paper›PMID 22745772›Full record

ArticlePloS one2012

Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.

Svetlana V Kalinichenko, Keiji Itoh, Elena V Korobko, Sergei Y Sokol, Vladimir L Buchman, Igor V Korobko

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
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  3. Review
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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 4 institutions in 3 countries.

Svetlana V KalinichenkoInstitute of Gene Biology, Russian Academy of Sciences, Moscow, Russia.
Keiji Itoh
Elena V Korobko
Sergei Y Sokol
Vladimir L Buchman
Igor V Korobko
Icahn School of Medicine at Mount Sinai · USRussian Academy of Sciences · RUCardiff University · GBInstitute of Gene Biology · RU

Funding

Wellcome TrustWellcome Trust 071269
6 · The paper itself

Abstract

MAK-V/Hunk is a scantily characterized AMPK-like protein kinase. Recent findings identified MAK-V as a pro-survival and anti-apoptotic protein and revealed its role in embryonic development as well as in tumorigenesis and metastasis. However molecular mechanisms of MAK-V action and regulation of its activity remain largely unknown. We identified Nedd4 as an interaction partner for MAK-V protein kinase. However, this HECT-type E3 ubiquitin ligase is not involved in the control of MAK-V degradation by the ubiquitin-proteasome system that regulates MAK-V abundance in cells. However, Nedd4 in an ubiquitin ligase-independent manner rescued developmental defects in Xenopus embryos induced by MAK-V overexpression, suggesting physiological relevance of interaction between MAK-V and Nedd4. This identifies Nedd4 as the first known regulator of MAK-V function.

Indexed as

AnimalsBlotting, WesternCycloheximideElectrophoresis, Polyacrylamide GelEndosomal Sorting Complexes Required for TransportHumansMiceNedd4 Ubiquitin Protein LigasesPC12 CellsProtein BindingProtein KinasesRatsUbiquitinationUbiquitin-Protein LigasesXenopus ProteinsCycloheximideEndosomal Sorting Complexes Required for TransportHUNK protein, ratNedd4l protein, mouseNEDD4L protein, ratnedd4l protein, XenopusNedd4 protein, humanNedd4 protein, ratNedd4 protein, XenopusNedd4 Ubiquitin Protein LigasesProtein KinasesUbiquitin-Protein LigasesXenopus Proteins

Identifiers

PMID22745772
PMCPMC3379983
OpenAlexW2071764780

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.