Evidence map›Paper›PMID 26898182›Full record

ReviewBiochimica et biophysica acta2016

VAP, a Versatile Access Point for the Endoplasmic Reticulum: Review and analysis of FFAT-like motifs in the VAPome.

Sarah E Murphy, Tim P Levine

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 194 papers.

0numbers the graph read from it
0cells of the map it votes in
194citing papers in PubMed
16.9field-weighted citation impact, top 1% 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

194 citing papers in PubMed, 333 citations in OpenAlex.

  1. Article
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  7. Peroxisome calcium uptake is dependent on ER-peroxisome membrane contact.Cellular and molecular life sciences : CMLS · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. VapA/Scs2 sustains polarized growth inMicrobial cell (Graz, Austria) · 2026
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025
    Review
  18. Article
  19. Article
  20. Article

134 more citing papers are in PubMed but not listed here.

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.

Sarah E MurphyDepartment of Cell Biology, UCL Institute of Ophthalmology, 11-43 Bath Street, UK EC1V 9EL.
Tim P LevineDepartment of Cell Biology, UCL Institute of Ophthalmology, 11-43 Bath Street, UK EC1V 9EL. Electronic address: tim.levine@ucl.ac.uk.
Institute of Ophthalmology · MX

Funding

Biotechnology and Biological Sciences Research Council BB/L016028Biotechnology and Biological Sciences Research Council BB/M011801Biotechnology and Biological Sciences Research Council BB/M011801/1
6 · The paper itself

Abstract

Dysfunction of VAMP-associated protein (VAP) is associated with neurodegeneration, both Amyotrophic Lateral Sclerosis and Parkinson's disease. Here we summarize what is known about the intracellular interactions of VAP in humans and model organisms. VAP is a simple, small and highly conserved protein on the cytoplasmic face of the endoplasmic reticulum (ER). It is the sole protein on that large organelle that acts as a receptor for cytoplasmic proteins. This may explain the extremely wide range of interacting partners of VAP, with components of many cellular pathways binding it to access the ER. Many proteins that bind VAP also target other intracellular membranes, so VAP is a component of multiple molecular bridges at membrane contact sites between the ER and other organelles. So far approximately 100 proteins have been identified in the VAP interactome (VAPome), of which a small minority have a "two phenylalanines in an acidic tract" (FFAT) motif as it was originally defined. We have analyzed the entire VAPome in humans and yeast using a simple algorithm that identifies many more FFAT-like motifs. We show that approximately 50% of the VAPome binds directly or indirectly via the VAP-FFAT interaction. We also review evidence on pathogenesis in genetic disorders of VAP, which appear to arise from reduced overall VAP levels, leading to ER stress. It is not possible to identify one single interaction that underlies disease. This article is part of a Special Issue entitled: The cellular lipid landscape edited by Tim P. Levine and Anant K. Menon.

Indexed as

Protein Interaction MapsAmino Acid MotifsAmino Acid SequenceAnimalsEndoplasmic ReticulumHumansMolecular Sequence DataProtein BindingProtein Interaction Domains and MotifsVesicular Transport ProteinsVAPA protein, humanVAPB protein, humanVesicular Transport ProteinsAmyotrophic Lateral Sclerosis/geneticsBiological TransportEndoplasmic Reticulum/*metabolismIntracellular Membranes/*metabolismMotor Neurons/*metabolismVesicular Transport Proteins/genetics/*metabolism

Identifiers

PMID26898182
OpenAlexW2277267665

What OpenQuestion holds

Textmetadata
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.