Evidence map›Paper›PMID 27458136›Full record

ArticleThe Journal of cell biology2016

Syntaxin-17 delivers PINK1/parkin-dependent mitochondrial vesicles to the endolysosomal system.

Gian-Luca McLelland, Sydney A Lee, Heidi M McBride, Edward A Fon

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 163 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
163citing papers in PubMed, 1 pooled it
14.8field-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

163 citing papers in PubMed, 1 synthesis or guideline pooled it, 238 citations in OpenAlex.

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103 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

4 authors at 1 institution in 1 country.

Gian-Luca McLellandMcGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada Neurodegenerative Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.
Sydney A LeeMcGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada Neurodegenerative Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.ORCID 0000-0002-8591-2062
Heidi M McBrideRare Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.ORCID 0000-0003-4666-2280
Edward A FonMcGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada Neurodegenerative Diseases Group, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada ted.fon@mcgill.ca.ORCID 0000-0002-5520-6239
Montreal Neurological Institute and Hospital · CA

Funding

CIHR
6 · The paper itself

Abstract

Mitochondria are considered autonomous organelles, physically separated from endocytic and biosynthetic pathways. However, recent work uncovered a PINK1/parkin-dependent vesicle transport pathway wherein oxidized or damaged mitochondrial content are selectively delivered to the late endosome/lysosome for degradation, providing evidence that mitochondria are indeed integrated within the endomembrane system. Given that mitochondria have not been shown to use canonical soluble NSF attachment protein receptor (SNARE) machinery for fusion, the mechanism by which mitochondrial-derived vesicles (MDVs) are targeted to the endosomal compartment has remained unclear. In this study, we identify syntaxin-17 as a core mitochondrial SNARE required for the delivery of stress-induced PINK1/parkin-dependent MDVs to the late endosome/lysosome. Syntaxin-17 remains associated with mature MDVs and forms a ternary SNARE complex with SNAP29 and VAMP7 to mediate MDV-endolysosome fusion in a manner dependent on the homotypic fusion and vacuole protein sorting (HOPS) tethering complex. Syntaxin-17 can be traced to the last eukaryotic common ancestor, hinting that the removal of damaged mitochondrial content may represent one of the earliest vesicle transport routes in the cell.

Indexed as

Amino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsCytoplasmic VesiclesEndosomesHumansLysosomesMiceMitochondriaMitophagyMultiprotein ComplexesPhagosomesProtein TransportQa-SNARE ProteinsSNARE ProteinsMultiprotein Complexesparkin proteinQa-SNARE ProteinsSNARE ProteinsUbiquitin-Protein Ligases

Identifiers

PMID27458136
PMCPMC4970327
OpenAlexW2483129460

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.