Evidence map›Paper›PMID 25557545›Full record

ArticleTraffic (Copenhagen, Denmark)2015

Atg27 tyrosine sorting motif is important for its trafficking and Atg9 localization.

Verónica A Segarra, Douglas R Boettner, Sandra K Lemmon

Open access · greenAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

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  14. Mechanisms governing autophagosome biogenesis.Nature reviews. Molecular cell biology · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Origin of the Autophagosome Membrane in Mammals.BioMed research international · 2018
    Review
  19. Review
  20. Article
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.

Verónica A SegarraDepartment of Molecular and Cellular Pharmacology, University of Miami, Miami, FL, USA.
Douglas R Boettner
Sandra K Lemmon
University of Miami · US

Funding

SUPPRESSORS OF CLATHRIN DEFICIENCY IN YEASTR01GM055796 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI LEMMON, SANDRA K. · 1998 to 2015
$4.7M
TRAINING PROGRAMS IN CARDIOVASCULAR PHARMACOLOGYT32HL007188 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SZCZESNA-CORDARY, DANUTA · 1985 to 2011
$3.8M
NHLBI NIH HHS T32 HL007188NHLBI NIH HHS T32-HL07188NIGMS NIH HHS R01 GM055796NIGMS NIH HHS R01-GM055796
6 · The paper itself

Abstract

During autophagy, the transmembrane protein Atg27 facilitates transport of the major autophagy membrane protein Atg9 to the preautophagosomal structure (PAS). To better understand the function of Atg27 and its relationship with Atg9, Atg27 trafficking and localization were examined. Atg27 localized to endosomes and the vacuolar membrane, in addition to previously described PAS, Golgi and Atg9-positive structures. Atg27 vacuolar membrane localization was dependent on the adaptor AP-3, which mediates direct transport from the trans-Golgi to the vacuole. The four C-terminal amino acids (YSAV) of Atg27 comprise a tyrosine sorting motif. Mutation of the YSAV abrogated Atg27 transport to the vacuolar membrane and affected its distribution in TGN/endosomal compartments, while PAS localization was normal. Also, in atg27(ΔYSAV) or AP-3 mutants, accumulation of Atg9 in the vacuolar lumen was observed upon autophagy induction. Nevertheless, PAS localization of Atg9 was normal in atg27(ΔYSAV) cells. The vacuole lumen localization of Atg9 was dependent on transport through the multivesicular body, as Atg9 accumulated in the class E compartment and vacuole membrane in atg27(ΔYSAV) vps4Δ but not in ATG27 vps4Δ cells. We suggest that Atg27 has an additional role to retain Atg9 in endosomal reservoirs that can be mobilized during autophagy.

Indexed as

Amino Acid MotifsAutophagyAutophagy-Related ProteinsCarrier ProteinsGolgi ApparatusMembrane ProteinsMultivesicular BodiesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTyrosineVacuolesVesicular Transport ProteinsATG27 protein, S cerevisiaeATG9 protein, S cerevisiaeAutophagy-Related ProteinsCarrier ProteinsMembrane ProteinsSaccharomyces cerevisiae ProteinsTyrosineVesicular Transport ProteinsAP-3Atg27Atg9autophagycytoplasm to vacuole transportendosomepreautophagosomal structuretrans-Golgi networktyrosine sorting motifvacuole

Identifiers

PMID25557545
PMCPMC5599220
OpenAlexW2101779902

What OpenQuestion holds

Textmetadata
LicenceTDM
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.