Evidence map›Paper›PMID 18801063›Full record

ReviewTraffic (Copenhagen, Denmark)2008

The TRAPP complex: insights into its architecture and function.

Michael Sacher, Yeon-Gil Kim, Arnon Lavie, Byung-Ha Oh, Nava Segev

Abstract readReview
In one paragraph

Review in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
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

65 citing papers in PubMed.

  1. Function and regulation of Rab GTPases in cancers.Cell biology and toxicology · 2024
    Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. The Role of Secretory Pathways inJournal of fungi (Basel, Switzerland) · 2020
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. The Journal of cell biology · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. TRAPP Complexes in Secretion and Autophagy.Frontiers in cell and developmental biology · 2016
    Review
  20. Tethering Complexes in the Arabidopsis Endomembrane System.Frontiers in cell and developmental biology · 2016
    Review

5 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

5 authors.

Michael SacherDepartment of Biology, Concordia University, Montreal, QC, Canada. msacher@alcor.concordia.ca
Yeon-Gil Kim
Arnon Lavie
Byung-Ha Oh
Nava Segev

Funding

YPTL GTPASE AND VESICULAR TRANSPORTR01GM045444 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SEGEV, NAVA · 1992 to 2020
$6.4M
NIGMS NIH HHS R01 GM045444
6 · The paper itself

Abstract

Vesicle-mediated transport is a process carried out by virtually every cell and is required for the proper targeting and secretion of proteins. As such, there are numerous players involved to ensure that the proteins are properly localized. Overall, transport requires vesicle budding, recognition of the vesicle by the target membrane and fusion of the vesicle with the target membrane resulting in delivery of its contents. The initial interaction between the vesicle and the target membrane has been referred to as tethering. Because this is the first contact between the two membranes, tethering is critical to ensuring that specificity is achieved. It is therefore not surprising that there are numerous 'tethering factors' involved ranging from multisubunit complexes, coiled-coil proteins and Rab guanosine triphosphatases. Of the multisubunit tethering complexes, one of the best studied at the molecular level is the evolutionarily conserved TRAPP complex. There are two forms of this complex: TRAPP I and TRAPP II. In yeast, these complexes function in a number of processes including endoplasmic reticulum-to-Golgi transport (TRAPP I) and an ill-defined step at the trans Golgi (TRAPP II). Because the complex was first reported in 1998 (1), there has been a decade of studies that have clarified some aspects of its function but have also raised further questions. In this review, we will discuss recent advances in our understanding of yeast and mammalian TRAPP at the structural and functional levels and its role in disease while trying to resolve some apparent discrepancies and highlighting areas for future study.

Indexed as

AnimalsGuanine Nucleotide Exchange FactorsHumansProtein BindingProtein Subunitsrab GTP-Binding ProteinsVesicular Transport ProteinsGuanine Nucleotide Exchange FactorsProtein Subunitsrab GTP-Binding Proteinstransport protein particle, TRAPPVesicular Transport Proteins

Identifiers

PMID18801063
PMCPMC3417770

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.