Evidence map›Paper›PMID 28007883›Full record

ArticleGenetics2017

Evidence for Amino Acid Snorkeling from a High-Resolution, In Vivo Analysis of Fis1 Tail-Anchor Insertion at the Mitochondrial Outer Membrane.

Abdurrahman Keskin, Emel Akdoğan, Cory D Dunn

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
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  3. Functional diversity in GII.4 norovirus entry: HBGA binding and capsid clustering dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  16. Article
  17. Mitochondrial proteins: from biogenesis to functional networks.Nature reviews. Molecular cell biology · 2019
    Review
  18. Article
  19. 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

3 authors at 1 institution in 2 countries.

Abdurrahman KeskinDepartment of Molecular Biology and Genetics, Koç University, 34450 Sarıyer, İstanbul, Turkey.
Emel AkdoğanDepartment of Molecular Biology and Genetics, Koç University, 34450 Sarıyer, İstanbul, Turkey.
Cory D DunnDepartment of Molecular Biology and Genetics, Koç University, 34450 Sarıyer, İstanbul, Turkey cdunn@ku.edu.tr.ORCID 0000-0003-2393-5944
Koç University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins localized to mitochondria by a carboxyl-terminal tail anchor (TA) play roles in apoptosis, mitochondrial dynamics, and mitochondrial protein import. To reveal characteristics of TAs that may be important for mitochondrial targeting, we focused our attention upon the TA of the Saccharomyces cerevisiae Fis1 protein. Specifically, we generated a library of Fis1p TA variants fused to the Gal4 transcription factor, then, using next-generation sequencing, revealed which Fis1p TA mutations inhibited membrane insertion and allowed Gal4p activity in the nucleus. Prompted by our global analysis, we subsequently analyzed the ability of individual Fis1p TA mutants to localize to mitochondria. Our findings suggest that the membrane-associated domain of the Fis1p TA may be bipartite in nature, and we encountered evidence that the positively charged patch at the carboxyl terminus of Fis1p is required for both membrane insertion and organelle specificity. Furthermore, lengthening or shortening of the Fis1p TA by up to three amino acids did not inhibit mitochondrial targeting, arguing against a model in which TA length directs insertion of TAs to distinct organelles. Most importantly, positively charged residues were more acceptable at several positions within the membrane-associated domain of the Fis1p TA than negatively charged residues. These findings, emerging from the first high-resolution analysis of an organelle targeting sequence by deep mutational scanning, provide strong, in vivo evidence that lysine and arginine can "snorkel," or become stably incorporated within a lipid bilayer by placing terminal charges of their side chains at the membrane interface.

Indexed as

Protein Sorting SignalsMitochondrial MembranesMitochondrial ProteinsMutationProtein DomainsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFIS1 protein, S cerevisiaeMitochondrial ProteinsProtein Sorting SignalsSaccharomyces cerevisiae Proteinsamino acid snorkelingdeep mutational scanningmembrane insertionmitochondrial divisionmitochondrial protein targeting

Identifiers

PMID28007883
PMCPMC5289845
OpenAlexW2561699263

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.