Evidence map›Paper›PMID 26787839›Full record

ArticleMolecular and cellular biology2016

An Outer Mitochondrial Translocase, Tom22, Is Crucial for Inner Mitochondrial Steroidogenic Regulation in Adrenal and Gonadal Tissues.

Maheshinie Rajapaksha, Jasmeet Kaur, Manoj Prasad, Kevin J Pawlak, Brendan Marshall, Elizabeth W Perry, Randy M Whittal, Himangshu S Bose

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.3field-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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Binaphthoquinone attenuates myofibroblast transition of human ventricular cardiac fibroblastsThe Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2026
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  4. Mitochondrial signal transduction.Cell metabolism · 2022
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  17. Endocrinology, diabetes & metabolism case reports · 2017
    Article
  18. Article
  19. ACTH Action on StAR Biology.Frontiers in neuroscience · 2016
    Review
  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

8 authors at 4 institutions in 2 countries.

Maheshinie RajapakshaDepartment of Biochemistry, Mercer University School of Medicine, Savannah, Georgia, USA.
Jasmeet KaurDepartment of Biochemistry, Mercer University School of Medicine, Savannah, Georgia, USA.
Manoj PrasadDepartment of Biochemistry, Mercer University School of Medicine, Savannah, Georgia, USA.
Kevin J PawlakDepartment of Biochemistry, Mercer University School of Medicine, Savannah, Georgia, USA.
Brendan MarshallDepartment of Cellular Biology and Anatomy, Georgia Regents University, Augusta, Georgia, USA.
Elizabeth W PerryDepartment of Cellular Biology and Anatomy, Georgia Regents University, Augusta, Georgia, USA.
Randy M WhittalDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.
Himangshu S BoseDepartment of Biochemistry, Mercer University School of Medicine, Savannah, Georgia, USA Anderson Cancer Institute, Memorial University Medical Center, Savannah, Georgia, USA bose_hs@mercer.edu.
Mercer University · USGeorgia Regents Medical Center · USMemorial Health University Medical Center · USUniversity of Alberta · CA

Funding

PHS HHS 057876
6 · The paper itself

Abstract

After cholesterol is transported into the mitochondria of steroidogenic tissues, the first steroid, pregnenolone, is synthesized in adrenal and gonadal tissues to initiate steroid synthesis by catalyzing the conversion of pregnenolone to progesterone, which is mediated by the inner mitochondrial enzyme 3β-hydroxysteroid dehydrogenase 2 (3βHSD2). We report that the mitochondrial translocase Tom22 is essential for metabolic conversion, as its knockdown by small interfering RNA (siRNA) completely ablated progesterone conversion in both steroidogenic mouse Leydig MA-10 and human adrenal NCI cells. Tom22 forms a 500-kDa complex with mitochondrial proteins associated with 3βHSD2. Although the absence of Tom22 did not inhibit mitochondrial import of cytochrome P450scc (cytochrome P450 side chain cleavage enzyme) and aldosterone synthase, it did inhibit 3βHSD2 expression. Electron microscopy showed that Tom22 is localized at the outer mitochondrial membrane (OMM), while 3βHSD2 is localized at the inner mitochondrial space (IMS), where it interacts through a specific region with Tom22 with its C-terminal amino acids and a small amino acid segment of Tom22 exposed to the IMS. Therefore, Tom22 is a critical regulator of steroidogenesis, and thus, it is essential for mammalian survival.

Indexed as

Adrenal GlandsAmino Acid SequenceAnimalsCell LineCells, CulturedDown-RegulationHumansLeydig CellsMaleMiceMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular Sequence DataProgesterone3 beta-hydroxysteroid dehydrogenase type IIMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProgesteroneProgesterone ReductaseRNA, Small InterferingTom22 protein, mouseTOMM22 protein, human

Identifiers

PMID26787839
PMCPMC4810470
OpenAlexW2290807655

What OpenQuestion holds

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Registered trials

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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.