Evidence map›Paper›PMID 20855891›Full record

ArticleThe Journal of biological chemistry2010

Identification of Ypk1 as a novel selective substrate for nitrogen starvation-triggered proteolysis requiring autophagy system and endosomal sorting complex required for transport (ESCRT) machinery components.

Mitsugu Shimobayashi, Hiromu Takematsu, Kazuo Eiho, Yukari Yamane, Yasunori Kozutsumi

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. TOR complex 2-Ypk1 signaling is an essential positive regulator of the general amino acid control response and autophagy.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  7. Article
  8. Article
  9. Need an ESCRT for autophagosomal maturation?Communicative & integrative biology · 2012
    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

5 authors.

Mitsugu ShimobayashiLaboratory of Membrane Biochemistry and Biophysics, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan.
Hiromu Takematsu
Kazuo Eiho
Yukari Yamane
Yasunori Kozutsumi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitrogen starvation-mediated reduction of Ypk1 is suggested to suppress translational initiation, possibly in parallel with the target of rapamycin complex 1 (TORC1) signaling. However, the molecular mechanism that regulates Ypk1 in nitrogen-starved cells is poorly understood. Here we report that Ypk1 is a novel selective substrate for nitrogen starvation-triggered proteolysis requiring autophagy system. Among various nutrient starvation methods used to elicit autophagy, rapid Ypk1 degradation was specific to nitrogen starvation. In screening genes required for such nitrogen starvation-specific vacuolar proteolysis, we found that autophagy-related degradation of Ypk1 depended on the endosomal sorting complex required for transport (ESCRT) machinery, which is conventionally thought to function in endosomal trafficking. In microscopic analyses, the disruption of ESCRT subunits resulted in the accumulation of both Ypk1 and autophagosomal Atg8 at a perivacuolar site that was distinct from conventional endosomes. ESCRT machinery was not involved in autophagic flux induced by the TORC1 inhibitor rapamycin, thus suggesting that ESCRT represents an exclusive mechanism of nitrogen starvation-specific proteolysis of Ypk1. Overall, we propose a novel regulation of Ypk1 that is specific to nitrogen limitation.

Indexed as

AutophagyBlotting, WesternEndosomal Sorting Complexes Required for TransportEndosomesGlycogen Synthase Kinase 3Microscopy, FluorescenceNitrogenPeptide HydrolasesProtein TransportReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionStarvationVacuolesEndosomal Sorting Complexes Required for TransportGlycogen Synthase Kinase 3MCK1 protein, S cerevisiaeNitrogenPeptide HydrolasesRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID20855891
PMCPMC2978627

What OpenQuestion holds

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Registered trials

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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.