Evidence map›Paper›PMID 22654911›Full record

ArticleInternational journal of cell biology2012

MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network.

Katie Marchbank, Sarah Waters, Roland G Roberts, Ellen Solomon, Caroline A Whitehouse

Open access · goldAbstract read
In one paragraph

Article in International journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Protein Aggregates and Aggrephagy in Myopathies.International journal of molecular sciences · 2023
    Review
  2. NBR1: The archetypal selective autophagy receptor.The Journal of cell biology · 2022
    Review
  3. ILRUN Promotes Atherosclerosis Through Lipid-Dependent and Lipid-Independent Factors.Arteriosclerosis, thrombosis, and vascular biology · 2022
    Article
  4. Article
  5. Article
  6. Circulation research · 2020
    Article
  7. Article
  8. Review
  9. Article
  10. Autophagy in adhesion and migration.Journal of cell science · 2016
    Review
  11. Article
  12. Article
  13. Autophagy and cancer.World journal of biological chemistry · 2013
    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 at 1 institution in 1 country.

Katie MarchbankDepartment of Medical and Molecular Genetics, Kings College London, London SE1 9RT, UK.
Sarah Waters
Roland G Roberts
Ellen Solomon
Caroline A Whitehouse
King's College London · GB

Funding

Arthritis Research UK 17655Medical Research Council MR/J006742/1Wellcome Trust
6 · The paper itself

Abstract

Selective autophagy is a process whereby specific targeted cargo proteins, aggregates, or organelles are sequestered into double-membrane-bound phagophores before fusion with the lysosome for protein degradation. It has been demonstrated that the microtubule network is important for the formation and movement of autophagosomes. Nbr1 is a selective cargo receptor that through its interaction with LC3 recruits ubiquitinated proteins for autophagic degradation. This study demonstrates an interaction between the evolutionarily conserved FW domain of Nbr1 with the microtubule-associated protein MAP1B. Upon autophagy induction, MAP1B localisation is focused into discrete vesicles with Nbr1. This colocalisation is dependent upon an intact microtubule network as depolymerisation by nocodazole treatment abolishes starvation-induced MAP1B recruitment to these vesicles. MAP1B is not recruited to autophagosomes for protein degradation as blockage of lysosomal acidification does not result in significant increased MAP1B protein levels. However, the protein levels of phosphorylated MAP1B are significantly increased upon blockage of autophagic degradation. This is the first evidence that links the ubiquitin receptor Nbr1, which shuttles ubiquitinated proteins to be degraded by autophagy, to the microtubule network.

Identifiers

PMID22654911
PMCPMC3357945
OpenAlexW2036983776

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.