Evidence map›Paper›PMID 27554484›Full record

ArticleeLife2016

Tim29 is a novel subunit of the human TIM22 translocase and is involved in complex assembly and stability.

Yilin Kang, Michael James Baker, Michael Liem, Jade Louber, Matthew McKenzie, Ishara Atukorala, Ching-Seng Ang, Shivakumar Keerthikumar, Suresh Mathivanan, Diana Stojanovski

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026
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  10. Proceedings of the National Academy of Sciences of the United States of America · 2023
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  18. Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021
    Review
  19. Article
  20. 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

10 authors at 3 institutions in 1 country.

Yilin KangDepartment of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Australia.
Michael James BakerDepartment of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Australia.
Michael LiemDepartment of Biochemistry and Genetics, La Trobe University, Melbourne, Australia.
Jade LouberDepartment of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Australia.
Matthew McKenzieCentre for Genetic Diseases, Hudson Institute of Medical Research, Melbourne, Australia.
Ishara AtukoralaDepartment of Biochemistry and Genetics, La Trobe University, Melbourne, Australia.
Ching-Seng AngThe Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, Australia.
Shivakumar KeerthikumarDepartment of Biochemistry and Genetics, La Trobe University, Melbourne, Australia.
Suresh MathivananDepartment of Biochemistry and Genetics, La Trobe University, Melbourne, Australia.
Diana StojanovskiDepartment of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Australia.ORCID 0000-0002-0199-3222
The University of Melbourne · AULa Trobe University · AUHudson Institute of Medical Research · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The TIM22 complex mediates the import of hydrophobic carrier proteins into the mitochondrial inner membrane. While the TIM22 machinery has been well characterised in yeast, the human complex remains poorly characterised. Here, we identify Tim29 (C19orf52) as a novel, metazoan-specific subunit of the human TIM22 complex. The protein is integrated into the mitochondrial inner membrane with it's C-terminus exposed to the intermembrane space. Tim29 is required for the stability of the TIM22 complex and functions in the assembly of hTim22. Furthermore, Tim29 contacts the Translocase of the Outer Mitochondrial Membrane, TOM complex, enabling a mechanism for transport of hydrophobic carrier substrates across the aqueous intermembrane space. Identification of Tim29 highlights the significance of analysing mitochondrial import systems across phylogenetic boundaries, which can reveal novel components and mechanisms in higher organisms.

Indexed as

Cell LineHumansMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProtein MultimerizationProtein SubunitsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProtein SubunitsTIMM29 protein, humanbiochemistrycell biologyhumanmitochondriaprotein traffickingTIM22

Identifiers

PMID27554484
PMCPMC5016092
OpenAlexW2514632080

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.