Evidence map›Paper›PMID 22740632›Full record

ArticleMolecular biology of the cell2012

NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum.

Ying Zhang, Uta Berndt, Hanna Gölz, Arlette Tais, Stefan Oellerer, Tina Wölfle, Edith Fitzke, Sabine Rospert

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 73 citations in OpenAlex.

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  12. Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021
    Review
  15. Review
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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

8 authors at 1 institution in 1 country.

Ying ZhangInstitute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, University of Freiburg, Freiburg, Germany.
Uta Berndt
Hanna Gölz
Arlette Tais
Stefan Oellerer
Tina Wölfle
Edith Fitzke
Sabine Rospert
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nascent polypeptide-associated complex (NAC) was initially found to bind to any segment of the nascent chain except signal sequences. In this way, NAC is believed to prevent mistargeting due to binding of signal recognition particle (SRP) to signalless ribosome nascent chain complexes (RNCs). Here we revisit the interplay between NAC and SRP. NAC does not affect SRP function with respect to signalless RNCs; however, NAC does affect SRP function with respect to RNCs targeted to the endoplasmic reticulum (ER). First, early recruitment of SRP to RNCs containing a signal sequence within the ribosomal tunnel is NAC dependent. Second, NAC is able to directly and tightly bind to nascent signal sequences. Third, SRP initially displaces NAC from RNCs; however, when the signal sequence emerges further, trimeric NAC·RNC·SRP complexes form. Fourth, upon docking to the ER membrane NAC remains bound to RNCs, allowing NAC to shield cytosolically exposed nascent chain domains not only before but also during cotranslational translocation. The combined data indicate a functional interplay between NAC and SRP on ER-targeted RNCs, which is based on the ability of the two complexes to bind simultaneously to distinct segments of a single nascent chain.

Indexed as

Dipeptidyl-Peptidases and Tripeptidyl-PeptidasesDNA-Binding ProteinsEndoplasmic ReticulumMolecular ChaperonesProtein BindingProtein BiosynthesisProtein TransportRibosomal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionSignal Recognition ParticleTranscription Factorsdipeptidyl peptidase IIDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDNA-Binding ProteinsEGD1 protein, S cerevisiaeMolecular Chaperonesnascent-polypeptide-associated complexribosomal protein L34Ribosomal ProteinsSaccharomyces cerevisiae ProteinsSignal Recognition ParticleTranscription Factors

Identifiers

PMID22740632
PMCPMC3418300
OpenAlexW2161002188

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.