Evidence map›Paper›PMID 12589064›Full record

ArticleMolecular biology of the cell2003

Mammalian ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domain.

Haruki Hasegawa, Sara Zinsser, Yeyoung Rhee, Einar Osland Vik-Mo, Svend Davanger, Jesse C Hay

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 83 citations in OpenAlex.

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  5. Sec22b is a critical and nonredundant regulator of plasma cell maintenance.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
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  8. Review
  9. A conformational switch driven by phosphorylation regulates the activity of the evolutionarily conserved SNARE Ykt6.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Conserved Oligomeric Golgi and Neuronal Vesicular Trafficking.Handbook of experimental pharmacology · 2018
    Review
  18. Article
  19. Article
  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

6 authors at 2 institutions in 2 countries.

Haruki HasegawaUniversity of Michigan, Department of Molecular, Cellular, and Developmental Biology, Ann Arbor 48109-1048, USA.
Sara Zinsser
Yeyoung Rhee
Einar Osland Vik-Mo
Svend Davanger
Jesse C Hay
University of Michigan · USUniversity of Bergen · NO

Funding

PROTEIN INTERACTIONS CONTROLLING ER/GOLGI TRANSPORTR01GM059378 · NIGMS · UNIVERSITY OF MONTANA · PI HAY, JESSE C · 1999 to 2010
$2.2M
NIGMS NIH HHS GM59378NIGMS NIH HHS R01 GM059378
6 · The paper itself

Abstract

SNAREs are required for specific membrane fusion throughout the endomembrane system. Here we report the characterization of rat ykt6, a prenylated SNARE selectively expressed in brain neurons. Immunofluorescence microscopy in neuronal and neuroendocrine cell lines revealed that membrane-associated ykt6 did not colocalize significantly with any conventional markers of endosomes, lysosomes, or the secretory pathway. However, ykt6-containing membranes displayed very minor overlaps with lysosomes and dense-core secretory granules and were similar to lysosomes in buoyant density. Thus, ykt6 appears to be specialized for the trafficking of a unique membrane compartment, perhaps related to lysosomes, involved in aspects of neuronal function. Targeting of this SNARE to the ykt6 compartment was mediated by its profilin-like amino-terminal domain, even in the absence of protein prenylation. Although several other R-SNAREs contain related amino-terminal domains, only the ykt6 version was able to confer the specialized localization. Rat ykt6, which contains an arginine in its SNARE motif zero-layer, was found to behave like other R-SNAREs in its SNARE assembly properties. Interestingly, cytosolic ykt6, constituting more than half of the total cellular pool, appeared to be conformationally inactive for SNARE complex assembly, perhaps indicative of a regulatory mechanism that prevents promiscuous and potentially deleterious SNARE interactions.

Indexed as

Contractile ProteinsVesicular Transport ProteinsAmino Acid MotifsAnimalsArginineBrainCell LineCell MembraneChickensCytoskeletonCytosolDNA, ComplementaryElectrophoresis, Polyacrylamide GelGlutathione TransferaseImmunohistochemistryLysosomesArginineContractile ProteinsDNA, ComplementaryGlutathione TransferaseMembrane ProteinsMicrofilament ProteinsPeptidesPfn1 protein, ratProfilinsR-SNARE ProteinsSNARE ProteinsVesicular Transport ProteinsYkt6 protein, rat

Identifiers

PMID12589064
PMCPMC150002
OpenAlexW2149645445

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.