Evidence map›Paper›PMID 27571067›Full record

ReviewInternational journal of molecular sciences2016

Multifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane Trafficking.

Masatoshi Maki, Terunao Takahara, Hideki Shibata

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
4.0field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.

  1. The protein interaction networks of mucolipins and two-pore channels.Biochimica et biophysica acta. Molecular cell research · 2019
    Pooled it
  2. bioRxiv : the preprint server for biology · 2026
    Article
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  5. Heavy metal-induced disruption of the autophagy-lysosomal pathway: implications for aging and neurodegenerative disorders.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
    Review
  6. Article
  7. Review
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  11. Mechanism and cellular function of direct membrane binding by the ESCRT and ERES-associated CaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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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

3 authors at 1 institution in 1 country.

Masatoshi MakiDepartment of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan. mmaki@agr.nagoya-u.ac.jp.
Terunao TakaharaDepartment of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan. takahara@agr.nagoya-u.ac.jp.
Hideki ShibataDepartment of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan. shibabou@agr.nagoya-u.ac.jp.
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ALG-2 (gene name: PDCD6) is a penta-EF-hand Ca(2+)-binding protein and interacts with a variety of proteins in a Ca(2+)-dependent fashion. ALG-2 recognizes different types of identified motifs in Pro-rich regions by using different hydrophobic pockets, but other unknown modes of binding are also used for non-Pro-rich proteins. Most ALG-2-interacting proteins associate directly or indirectly with the plasma membrane or organelle membranes involving the endosomal sorting complex required for transport (ESCRT) system, coat protein complex II (COPII)-dependent ER-to-Golgi vesicular transport, and signal transduction from membrane receptors to downstream players. Binding of ALG-2 to targets may induce conformational change of the proteins. The ALG-2 dimer may also function as a Ca(2+)-dependent adaptor to bridge different partners and connect the subnetwork of interacting proteins.

Indexed as

AnimalsApoptosis Regulatory ProteinsBiological TransportCalciumCalcium-Binding ProteinsCell MembraneEndosomal Sorting Complexes Required for TransportHumansMultivesicular BodiesProtein BindingApoptosis Regulatory ProteinsCalciumCalcium-Binding ProteinsEndosomal Sorting Complexes Required for TransportPDCD6 protein, humanALG-2ALIXcalciumCOPIIESCRTmembrane repairmultivesicular bodyPDCD6protein–protein interactionSec31A

Identifiers

PMID27571067
PMCPMC5037681
OpenAlexW2512606991

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.