Evidence map›Paper›PMID 26272916›Full record

ArticleJournal of cell science2015

mRNA encoding Sec61β, a tail-anchored protein, is localized on the endoplasmic reticulum.

Xianying A Cui, Hui Zhang, Lena Ilan, Ai Xin Liu, Iryna Kharchuk, Alexander F Palazzo

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2015. 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
0.6field-weighted citation impact, top 30% 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, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Nesprin-2 Interacts with Condensin Component SMC2.International journal of cell biology · 2017
    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 1 country.

Xianying A CuiUniversity of Toronto, Department of Biochemistry, 1 King's College Circle, MSB Room 5336, Toronto, ON, M5S 1A8, Canada.
Hui ZhangUniversity of Toronto, Department of Biochemistry, 1 King's College Circle, MSB Room 5336, Toronto, ON, M5S 1A8, Canada.
Lena IlanUniversity of Toronto, Department of Biochemistry, 1 King's College Circle, MSB Room 5336, Toronto, ON, M5S 1A8, Canada.
Ai Xin LiuUniversity of Toronto, Department of Biochemistry, 1 King's College Circle, MSB Room 5336, Toronto, ON, M5S 1A8, Canada.
Iryna KharchukUniversity of Toronto, Department of Biochemistry, 1 King's College Circle, MSB Room 5336, Toronto, ON, M5S 1A8, Canada.
Alexander F PalazzoUniversity of Toronto, Department of Biochemistry, 1 King's College Circle, MSB Room 5336, Toronto, ON, M5S 1A8, Canada alex.palazzo@utoronto.ca.
Canada Research Chairs · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although one pathway for the post-translational targeting of tail-anchored proteins to the endoplasmic reticulum (ER) has been well defined, it is unclear whether additional pathways exist. Here, we provide evidence that a subset of mRNAs encoding tail-anchored proteins, including Sec61β and nesprin-2, is partially localized to the surface of the ER in mammalian cells. In particular, Sec61b mRNA can be targeted to, and later maintained on, the ER using both translation-dependent and -independent mechanisms. Our data suggests that this process is independent of p180 (also known as RRBP1), a known mRNA receptor on the ER, and the transmembrane domain recognition complex (TRC) pathway components, TRC40 (also known as ASNA1) and BAT3 (also known as BAG6). In addition, our data indicates that Sec61b mRNA might access translocon-bound ribosomes. Our results show that certain tail-anchored proteins are likely to be synthesized directly on the ER, and this facilitates their membrane insertion. Thus, it is clear that mammalian cells utilize multiple mechanisms to ensure efficient targeting of tail-anchored proteins to the surface of the ER.

Indexed as

AnimalsCarrier ProteinsChlorocebus aethiopsCOS CellsEndoplasmic ReticulumHumansMembrane ProteinsMicrofilament ProteinsNerve Tissue ProteinsNuclear ProteinsProtein TransportReceptors, Cytoplasmic and NuclearRNA, MessengerSEC Translocation ChannelsCarrier ProteinsMembrane ProteinsMicrofilament ProteinsNerve Tissue ProteinsNuclear ProteinsReceptors, Cytoplasmic and NuclearRNA, MessengerRRBP1 protein, humanSEC61B protein, humanSEC Translocation ChannelsSYNE2 protein, humanEndoplasmic reticulummRNA localizationSecretionTail-anchored protein

Identifiers

PMID26272916
PMCPMC4582399
OpenAlexW2169531456

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.