Evidence map›Paper›PMID 26055714›Full record

ArticleThe Journal of biological chemistry2015

Tid1, the Mammalian Homologue of Drosophila Tumor Suppressor Tid56, Mediates Macroautophagy by Interacting with Beclin1-containing Autophagy Protein Complex.

Ge Niu, Huan Zhang, Dan Liu, Li Chen, Chandra Belani, Hong-Gang Wang, Hua Cheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.4field-weighted citation impact, top 33% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Analysis of theCells · 2024
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. The one thousand and one chaperones of the NF-κB pathway.Cellular and molecular life sciences : CMLS · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Aging · 2019
    Article
  13. Article
  14. Review
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

7 authors at 2 institutions in 1 country.

Ge NiuInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Huan ZhangInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Dan LiuInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Li ChenInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Chandra BelaniPenn State Hershey Cancer Institute, Penn State University College of Medicine, Hershey, Pennsylvania 17033.
Hong-Gang WangPenn State Hershey Cancer Institute, Penn State University College of Medicine, Hershey, Pennsylvania 17033.
Hua ChengInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201; Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201; Departments of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, Maryland 21201; Departments of Medicine, University of Maryland School of Medicine, Baltimore, Maryland 21201. Electronic address: hcheng@ihv.umaryland.edu.
University of Maryland, Baltimore · USPenn State Milton S. Hershey Medical Center · US

Funding

Linking IKKbeta activation to anti-autophagy in viral protein Tax-mediated oncogeR01AI090113 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI CHENG, HUA · 2010 to 2013
$1.5M
NIAID NIH HHS R01 AI090113NIAID NIH HHS R01AI090113
6 · The paper itself

Abstract

One of the fundamental functions of molecular chaperone proteins is to selectively conjugate cellular proteins, targeting them directly to lysosome. Some of chaperones, such as the stress-induced Hsp70, also play important roles in autophagosome-forming macroautophagy under various stress conditions. However, the role of their co-chaperones in autophagy regulation has not been well defined. We here show that Tid1, a DnaJ co-chaperone for Hsp70 and the mammalian homologue of the Drosophila tumor suppressor Tid56, is a key mediator of macroautophagy pathway. Ectopic expression of Tid1 induces autophagy by forming LC3+ autophagosome foci, whereas silencing Tid1 leads to drastic impairment of autophagy as induced by nutrient deprivation or rapamycin. In contrast, Hsp70 is dispensable for a role in nutrient deprivation-induced autophagy. The murine Tid1 can be replaced with human Tid1 in murine fibroblast cells for induction of autophagy. We further show that Tid1 increases autophagy flux by interacting with the Beclin1-PI3 kinase class III protein complex in response to autophagy inducing signal and that Tid1 is an essential mediator that connects IκB kinases to the Beclin1-containing autophagy protein complex. Together, these results reveal a crucial role of Tid1 as an evolutionarily conserved and essential mediator of canonical macroautophagy.

Indexed as

AutophagyAnimalsApoptosis Regulatory ProteinsBeclin-1Cell LineDrosophilaDrosophila ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansI-kappa B KinaseMembrane ProteinsMiceMitochondrial ProteinsProtein Interaction MapsApoptosis Regulatory ProteinsBeclin-1BECN1 protein, humanCG5504 protein, DrosophilaDNAJA3 protein, humanDrosophila ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsI-kappa B KinaseMembrane ProteinsMitochondrial Proteins70 kilodalton heat shock protein (Hsp70)autophagyBeclin-1 (BECN1)chaperone DnaJ (DnaJ)molecular chaperonePI3KC3Tid1

Identifiers

PMID26055714
PMCPMC4505055
OpenAlexW1562750257

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.