Evidence map›Paper›PMID 33826365›Full record

ArticleMolecular biology of the cell2021

RTN4B interacting protein FAM134C promotes ER membrane curvature and has a functional role in autophagy.

Darshan Kumar, Behnam Lak, Taina Suntio, Helena Vihinen, Ilya Belevich, Tiina Viita, Liu Xiaonan, Aki Vartiainen, Maria Vartiainen, Markku Varjosalo and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.0field-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

23 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

11 authors at 2 institutions in 3 countries.

Darshan KumarCell and Tissue Dynamics Research Program.
Behnam LakCell and Tissue Dynamics Research Program.
Taina SuntioCell and Tissue Dynamics Research Program.
Helena VihinenCell and Tissue Dynamics Research Program.
Ilya BelevichCell and Tissue Dynamics Research Program.
Tiina ViitaCell and Tissue Dynamics Research Program.
Liu XiaonanMolecular Systems Biology Research Group and Proteomics Unit, Institute of Biotechnology, Helsinki Institute of Life Science, University of Helsinki, 00014 Helsinki, Finland.
Aki VartiainenCell and Tissue Dynamics Research Program.
Maria VartiainenCell and Tissue Dynamics Research Program.
Markku VarjosaloMolecular Systems Biology Research Group and Proteomics Unit, Institute of Biotechnology, Helsinki Institute of Life Science, University of Helsinki, 00014 Helsinki, Finland.
Eija JokitaloCell and Tissue Dynamics Research Program.
Tissue Dynamics (Israel) · ILUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is composed of a controlled ratio of sheets and tubules, which are maintained by several proteins with multiple functions. Reticulons (RTNs), especially RTN4, and DP1/Yop1p family members are known to induce ER membrane curvature. RTN4B is the main RTN4 isoform expressed in nonneuronal cells. In this study, we identified FAM134C as a RTN4B interacting protein in mammalian, nonneuronal cells. FAM134C localized specifically to the ER tubules and sheet edges. Ultrastructural analysis revealed that overexpression of FAM134C induced the formation of unbranched, long tubules or dense globular structures composed of heavily branched narrow tubules. In both cases, tubules were nonmotile. ER tubulation was dependent on the reticulon homology domain (RHD) close to the N-terminus. FAM134C plays a role in the autophagy pathway as its level elevated significantly upon amino acid starvation but not during ER stress. Moreover, FAM134C depletion reduced the number and size of autophagic structures and the amount of ER as a cargo within autophagic structures under starvation conditions. Dominant-negative expression of FAM134C forms with mutated RHD or LC3 interacting region also led to a reduced number of autophagic structures. Our results suggest that FAM134C provides a link between regulation of ER architecture and ER turnover by promoting ER tubulation required for subsequent ER fragmentation and engulfment into autophagosomes.

Indexed as

AutophagyAutophagy-Related ProteinsCell LineEndoplasmic ReticulumHEK293 CellsHeLa CellsHumansMembrane ProteinsNogo ProteinsProtein DomainsAutophagy-Related ProteinsMembrane ProteinsNogo ProteinsRETREG3 protein, humanRTN4 protein, human

Identifiers

PMID33826365
PMCPMC8351555
OpenAlexW3150790972

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.