Affinage

TOMM22

Mitochondrial import receptor subunit TOM22 homolog · UniProt Q9NS69

Length
142 aa
Mass
15.5 kDa
Annotated
2026-04-28
45 papers in source corpus 26 papers cited in narrative 26 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TOMM22 is the central organizer and presequence receptor of the mitochondrial translocase of the outer membrane (TOM) complex, coordinating precursor protein recognition, channel gating, and higher-order complex assembly. Its cytosolic domain—a three-helix bundle structurally similar to Tom20—binds presequence-carrying precursors and hands them to the IMS domain, which transfers them to Tim50 of the TIM23 inner-membrane translocase, establishing a relay across the outer membrane (PMID:21896724, PMID:35733257, PMID:9252394). Phosphorylation by CK2 (Ser44/Ser46) promotes Tom22 import and controls PINK1-dependent mitophagy in skeletal muscle, CK1 (Thr57) stimulates its assembly with Tom20, and PKA (Thr76) opposes import, while porin/VDAC acts as a chaperone sink regulating Tom22 integration into the trimeric TOM complex (PMID:24093680, PMID:29165030, PMID:30738703). Beyond protein import, TOMM22 serves as the mitochondrial receptor for pro-apoptotic Bax—recognizing its GALLL motif and stimulating C-terminal helix membrane insertion—and participates in steroidogenic complexes with 3βHSD2 and aldosterone synthase (PMID:17096026, PMID:39043635, PMID:26787839).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1997 High

    Establishing that Tom22 functions as an independent presequence receptor—not merely a structural subunit—answered the question of how preproteins are recognized at the outer membrane beyond Tom20 and Tom70.

    Evidence In vitro binding assays with purified recombinant cytosolic domains and presequence competition in yeast

    PMID:9252394

    Open questions at the time
    • Binding affinity constants for different presequence classes not determined
    • Relative contributions of Tom20 vs Tom22 to different precursor classes unclear
  2. 1997 High

    Demonstrating that the IMS domain of Tom22 acts as a trans binding site for preproteins established a vectorial relay mechanism (acid chain hypothesis) for precursor transfer across the outer membrane.

    Evidence Import assays with IMS domain deletion mutants in yeast mitochondria

    PMID:9343421

    Open questions at the time
    • Identity of the trans-side acceptor partner (later shown to be Tim50) was unknown
    • How the IMS domain discriminates different precursor classes was not resolved
  3. 1998 High

    Defining a positively charged internal import signal in Tom22's cytosolic domain, separate from the transmembrane anchor, revealed how this outer-membrane protein is itself targeted to mitochondria.

    Evidence In vitro import assays with deletion and charge-reversal mutants of Neurospora TOM22

    PMID:9565567

    Open questions at the time
    • Whether the same import signal mechanism operates in mammalian Tom22 was not tested
  4. 1999 High

    Genetic deletion of Tom22 showed it is the central organizer of the TOM complex: its transmembrane domain stabilizes higher-order architecture and its cytosolic domain docks Tom20 and Tom70, resolving whether Tom22 is merely a receptor or a structural scaffold.

    Evidence Yeast tom22Δ strain analyzed by BN-PAGE, import assays, and channel electrophysiology

    PMID:10519552

    Open questions at the time
    • Structural basis for how Tom22 TMD mediates complex stability was unknown
    • How Tom22 influences channel gating at the molecular level remained unresolved
  5. 2000 High

    Identification of mammalian TOM22 as a functional homolog—co-assembling with TOM40, inhibiting import when blocked by antibodies, and complementing yeast Δtom22—extended the receptor/organizer paradigm to higher eukaryotes.

    Evidence Immunopurification, BN-PAGE, antibody inhibition, and yeast complementation in mammalian/yeast systems

    PMID:10900208 PMID:10982837

    Open questions at the time
    • Structural differences between fungal and mammalian Tom22 not resolved
    • Whether mammalian Tom22 IMS domain has the same trans-binding function was untested
  6. 2001 High

    Demonstrating that Tom40 and Tom22 form a urea-resistant core (GIP complex) containing two coupled channel pores clarified the minimal translocation-competent unit and the essential role of Tom22 in maintaining dual-pore architecture.

    Evidence Detergent solubilization, BN-PAGE, preprotein arrest assays, and electrophysiology of purified GIP complex

    PMID:11259583

    Open questions at the time
    • Stoichiometry and atomic contacts between Tom22 and Tom40 in the core unknown
  7. 2006 High

    Identifying TOM22 as the mitochondrial receptor for pro-apoptotic Bax—with antibody blockade inhibiting Bax-dependent apoptosis—revealed that the import receptor moonlights in apoptosis regulation.

    Evidence Bacterial two-hybrid, crosslinking, peptide mapping, antibody inhibition, and antisense knockdown

    PMID:17096026

    Open questions at the time
    • Whether Tom22-Bax interaction competes with preprotein import was not determined
    • Structural basis of the interaction unknown
  8. 2011 High

    In vivo photocrosslinking at single-residue resolution demonstrated that Tom22's cytosolic domain accepts precursors from Tom20 and its IMS domain hands them to Tim50, completing the relay model from receptor to inner-membrane translocase.

    Evidence Site-specific photocrosslinking in intact yeast mitochondria with substrate competition controls

    PMID:21896724

    Open questions at the time
    • Kinetics of the handoff reaction not established
    • Whether all precursor classes use the same relay path unclear
  9. 2013 High

    Mapping three phosphorylation sites (CK2-Ser44/46, CK1-Thr57, PKA-Thr76) with opposing effects on Tom22 import and TOM assembly established kinase-mediated metabolic regulation of outer-membrane translocase biogenesis.

    Evidence Mass spectrometry phospho-mapping, in vitro kinase assays, import assays, and BN-PAGE assembly in yeast

    PMID:24093680

    Open questions at the time
    • How phosphorylation status is sensed during metabolic transitions in vivo not fully resolved
    • Whether additional kinases contribute was not excluded
  10. 2016 Medium

    Tom22 was shown to be essential for steroidogenesis, forming a ~500 kDa complex with 3βHSD2 via its IMS-exposed C-terminal residues, revealing an unexpected specialized function beyond general protein import.

    Evidence siRNA knockdown, BN-PAGE, Co-IP, mass spectrometry in adrenal/gonadal cells

    PMID:26787839

    Open questions at the time
    • Single lab observation; independent replication needed
    • Mechanism by which Tom22 supports 3βHSD2 expression unknown
  11. 2017 High

    Demonstrating that the IMS AAA protease Yme1 degrades Tom22 by dislocating its cytoplasmic domain into the IMS identified the quality-control pathway for an outer-membrane TOM subunit, an unusual topological inversion during proteolysis.

    Evidence Immunoprecipitation, in vivo photocrosslinking, and ATPase-dead mutant analysis in yeast

    PMID:29138251

    Open questions at the time
    • Signals triggering Yme1-mediated Tom22 degradation not identified
    • Whether this pathway operates in mammalian cells unknown
  12. 2018 High

    CK2-dependent phosphorylation of TOMM22 was shown to control PINK1-dependent mitophagy in mammalian muscle: loss of phosphorylation accumulates PINK1 and induces mitophagy, linking Tom22 receptor function to mitochondrial quality control in vivo.

    Evidence Skeletal muscle-specific Csnk2b knockout mice, phosphomimetic rescue, electron microscopy, OCR measurement

    PMID:29165030

    Open questions at the time
    • Which TOMM22 phosphosite(s) are critical for PINK1 import not pinpointed
    • Relevance to non-muscle tissues not tested
  13. 2019 High

    Porin/VDAC was identified as a chaperone sink that sequesters newly imported Tom22, modulating the balance between trimeric (Tom22-containing) and dimeric TOM complexes and thereby tuning import pathway selectivity.

    Evidence Reciprocal Co-IP, in vivo photocrosslinking, BN-PAGE, and import assays in yeast

    PMID:30738703

    Open questions at the time
    • Structural basis of Porin-Tom22 interaction unknown
    • How the cell regulates the sink capacity of Porin not established
  14. 2022 High

    Near-atomic cryo-EM structures of the human TOM complex revealed that Tom22's cytosolic domain is a three-helix bundle similar to Tom20, with helix H1 critical for presequence binding, providing the first structural framework for receptor–presequence recognition.

    Evidence Cryo-EM at 2.53 Å and 3.74 Å resolution with structure-guided mutagenesis and presequence binding assays

    PMID:35733257

    Open questions at the time
    • Structure of Tom22 in complex with a bound presequence peptide not obtained
    • Dynamics of receptor engagement during translocation not captured
  15. 2024 High

    Cell-free nanodisc reconstitution demonstrated that Tom22 directly stimulates Bax membrane insertion by recognizing the GALLL motif in helix α1 and triggering C-terminal helix α9 extrusion, mechanistically resolving the Tom22-Bax apoptotic interaction.

    Evidence Nanodisc reconstitution, site-directed mutagenesis, liposome permeabilization assay

    PMID:39043635

    Open questions at the time
    • Whether other TOM subunits modulate this activity in the native complex not tested
    • In vivo validation in a mammalian apoptosis model not performed

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include: how Tom22 dynamics mechanistically gate the Tom40 channel (computational evidence only), the phosphorylation-site specificity controlling PINK1 import, the structural basis of Tom22's steroidogenic complexes, and whether Yme1-mediated Tom22 degradation is conserved in mammals.
  • No experimental validation of simulated Tom22-Tom40 gating coupling
  • Phosphosite specificity for PINK1 import regulation unresolved
  • Yme1-Tom22 axis not tested in mammalian systems

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0038024 cargo receptor activity 8 GO:0060090 molecular adaptor activity 4 GO:0005198 structural molecule activity 2 GO:0044183 protein folding chaperone 1
Localization
GO:0043226 organelle 5 GO:0005886 plasma membrane 3
Pathway
R-HSA-9609507 Protein localization 6 R-HSA-392499 Metabolism of proteins 4 R-HSA-5357801 Programmed Cell Death 3 R-HSA-1430728 Metabolism 2 R-HSA-9612973 Autophagy 1
Partners
BAXCYP11B2HSD3B2TIMM50TOMM20TOMM40TOMM70VDAC1
Complex memberships
3βHSD2-Tom22 steroidogenic complexGIP complex (Tom40-Tom22 core)TOM complex

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 Tom22 is a multifunctional organizer of the TOM complex: its single transmembrane domain stabilizes interactions between core TOM complexes, its cytosolic domain serves as a docking point for peripheral receptors Tom20 and Tom70, and its absence causes dissociation of the translocase into core complexes and loss of tight channel gating control. Genetic deletion (yeast tom22Δ strain), blue native PAGE, import assays, channel electrophysiology Nature High 10519552
1997 The purified cytosolic domain of Tom22 selectively recognizes presequence-carrying preproteins in a salt-sensitive manner and competes with presequence peptides for binding, establishing Tom22 as an independent presequence receptor distinct from Tom20 and Tom70. In vitro binding assay with purified recombinant cytosolic domains; competition with synthetic presequence peptides The Journal of biological chemistry High 9252394
1997 The intermembrane space (IMS) domain of Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences; removal of cytosolic receptor domains unmasks a strict requirement for the IMS domain, supporting the acid chain hypothesis of sequential cis-to-trans preprotein transfer. Import assays with mutant mitochondria lacking IMS domain of Tom22; two-step import protocol (accumulation then membrane potential re-establishment) Molecular and cellular biology High 9343421
1999 Tom22 binds to segments corresponding to the C-terminal part of the presequence and the N-terminal part of the mature protein of a cleavable preprotein (CoxIV), while Tom70 and Tom20 bind multiple segments of non-cleavable preproteins (phosphate carrier), revealing differential binding site distributions for the three receptors. Cellulose-bound peptide scans (13-mer peptide libraries) with purified cytosolic receptor domains The Journal of biological chemistry High 10347216
2001 Tom40 and Tom22 together form the highly stable core unit of the GIP complex that retains accumulated preproteins; the complex contains two simultaneously active coupled channel pores and is resistant to urea and alkaline pH, with preprotein binding independent of ionic interactions. Detergent solubilization, BN-PAGE, preprotein arrest assays, electrophysiology of purified GIP complex Molecular and cellular biology High 11259583
2006 TOM22 acts as a mitochondrial receptor for pro-apoptotic Bax; the interaction involves the first alpha helix of Bax and central pore-forming helices; antibody blockade or antisense knockdown of TOM22 inhibits Bax mitochondrial association and Bax-dependent apoptosis. Bacterial two-hybrid, crosslinking, peptide mapping, antibody inhibition, antisense knockdown Cell death and differentiation High 17096026
2007 Tom20 and Tom22 are involved in the same sequential step of targeting signal recognition; deletion of the receptor domain of either Tom20 or Tom22 in isolated yeast mitochondria produces nearly identical import defects across diverse mitochondrial precursor proteins. In vitro protease cleavage of receptor domains via introduced TEV sites; import assays of diverse precursors The Journal of biological chemistry High 18063580
2011 In vivo site-specific photocrosslinking revealed that Tom22's cytosolic domain accepts substrate precursor proteins from Tom20, while its IMS domain transfers them to Tim50 of the inner-membrane TIM23 translocator, defining a handoff relay across the outer membrane. In vivo and in organello site-specific photocrosslinking at single amino acid resolution Proceedings of the National Academy of Sciences of the United States of America High 21896724
2000 Human TOM22 (hTom22) forms a complex with Tom20, its cytosolic domain functions as an import receptor, the C-terminal segment of the cytosolic domain binds presequences, the N-terminal domain binds the mature portion of preproteins, and an internal segment of the cytosolic domain mediates interaction with Tom20. Import inhibition assays with deletion mutants, cell-free immunoprecipitation, binding studies with pOTC derivatives Molecular and cellular biology High 10982837
2000 Mammalian TOM22 (1C9-2) is a functional homolog of fungal Tom22: it co-assembles with TOM40 in the ~400-kDa TOM complex, antibodies against it inhibit preprotein import into isolated mitochondria, and it complements growth and import defects of yeast Δtom22 cells. Immunopurification, BN-PAGE, import inhibition with antibodies, yeast complementation The Journal of biological chemistry High 10900208
2013 Three kinases regulate Tom22 import and assembly: CK2 constitutively phosphorylates cytosolic precursor Tom22 at Ser44/Ser46 promoting its import; CK1 (bound to mitochondria, glucose-induced) phosphorylates Tom22 at Thr57 stimulating assembly of Tom22 and Tom20; PKA (glucose-activated) phosphorylates Tom22 at Thr76 and impairs its import, acting oppositely to CK1 and CK2. In vitro kinase assays, mass spectrometry phospho-mapping, import assays, BN-PAGE assembly analysis Cell metabolism High 24093680
2018 In mammalian skeletal muscle, CSNK2/CK2-mediated phosphorylation of TOMM22 controls mitophagy: loss of Csnk2b reduces TOMM22 phosphorylation, changes its binding affinity for precursor proteins, accumulates PINK1 on mitochondria, and induces mitophagy; phosphomimetic TOMM22 rescues mitophagy and oxygen consumption rate. Skeletal muscle-specific Csnk2b conditional knockout mice, in vitro phosphorylation assay, electron microscopy (autophagosome detection), electroporation of phosphomimetic constructs, oxygen consumption rate measurement Autophagy High 29165030
2019 Porin (Por1/VDAC) associates with newly imported Tom22 to act as a chaperone sink, modulating Tom22 integration into the trimeric TOM complex; Por1 sequestration of Tom22 also enhances the dimeric TOM complex (lacking Tom22), which preferentially imports TIM40/MIA-dependent proteins. Co-immunoprecipitation, BN-PAGE, in vivo photocrosslinking, import assays, Tom6 phosphorylation cell-cycle analysis Molecular cell High 30738703
2022 Cryo-EM structure of the human TOM core complex at 2.53 Å and the TOM complex with Tom22 and Tom20 cytosolic domains at 3.74 Å reveals that Tom20 and Tom22 share a similar three-helix bundle in their cytosolic domains; structure-guided mutagenesis shows the Tom22 cytosolic domain binds presequences and helix H1 is critical for this binding. Cryo-EM structure determination, structure-guided mutagenesis, presequence binding assays Proceedings of the National Academy of Sciences of the United States of America High 35733257
1998 A short segment of the cytosolic domain of TOM22 bearing a net positive charge serves as an internal import signal required for targeting and correct outer-membrane insertion; this signal is physically separate from the transmembrane anchor; altering its charge impairs import. In vitro import assays with deletion and charge-reversal mutants of Neurospora TOM22 The Journal of biological chemistry High 9565567
2004 Rat TOM22 targeting and TOM complex integration requires three distinct structural elements: a cytoplasmic 10-residue acidic alpha-helical import sequence ~30 residues upstream of the TMD, the TMD with appropriate hydrophobicity, and a 20-residue C-terminal signal; the import sequence interacts intramolecularly with the TMD and C-tail and also with Tom20. Confocal microscopy and cell fractionation of HeLa cells expressing deletion/mutation constructs; BN-PAGE; yeast two-hybrid The Journal of biological chemistry High 14985332
2003 The cytosolic domain of Tom22 has chaperone-like activity, suppressing aggregation of unfolded citrate synthase; this activity is inhibitable by a presequence peptide, suggesting the presequence binding site overlaps with the chaperone active site. In vitro aggregation suppression assay with purified cytosolic domains; presequence competition The Journal of biological chemistry Medium 14699115
2017 The mitochondrial inner-membrane AAA protease Yme1 degrades outer-membrane Tom22 from the IMS side; the Yme1 adaptors Mgr1 and Mgr3 recognize the IMS domain of Tom22, and Yme1's ATPase activity dislocates Tom22's cytoplasmic domain into the IMS for proteolysis. Immunoprecipitation, in vivo site-specific photocrosslinking, ATPase mutant analysis The Journal of cell biology High 29138251
2018 Yeast TOMM22 (Tom22) acts as the main receptor for amyloid-β (Aβ) peptides at mitochondria; Aβ residues 25-42 mediate the specific interaction with Tom22; Aβ is then transferred to Tom40 for translocation into the mitochondrial matrix. Yeast genetic deletion, binding assays with Aβ peptide truncations, import competition The Journal of biological chemistry Medium 29925587
2016 Tom22 is essential for steroidogenesis in adrenal and gonadal tissues: siRNA knockdown ablates progesterone synthesis; Tom22 forms a ~500-kDa complex with 3βHSD2 at the IMS, interacting via its IMS-exposed C-terminal residues, and is required for 3βHSD2 expression but not for import of CYP450scc or aldosterone synthase. siRNA knockdown, blue native gel electrophoresis, Co-IP, mass spectrometry, electron microscopy localization Molecular and cellular biology Medium 26787839
2021 Tom22 forms a trimolecular 110-kDa complex with aldosterone synthase (P450c11AS) and intramitochondrial 30-kDa StAR in the stressed rat heart, required for intracardiac aldosterone synthesis; this is the first ascribed function for intramitochondrial 30-kDa StAR. Blue native gel electrophoresis, immunoblotting, protein crosslinking, co-immunoprecipitation, mass spectrometry The Journal of pharmacology and experimental therapeutics Medium 33526603
2010 TOMM22 is specifically required for hepatocyte survival in zebrafish; loss-of-function mutation leads to hepatocyte-specific death after differentiation without affecting bile duct formation, demonstrating a tissue-specific requirement for mitochondrial protein import. Forward genetic screen, zebrafish tomm22 mutant, morpholino knockdown, histology Disease models & mechanisms Medium 20483998
2011 The cytosolic domain of human Tom22 modulates the conformation of pro-apoptotic Bax upon mitochondrial interaction: expression of this domain increases Bax mitochondrial localization but decreases the proportion of active Bax and interferes with Bax oligomerization. Co-immunoprecipitation, BN-PAGE, yeast expression system FEBS letters Medium 22198199
2019 Tom22 modulates mitochondrial fusion by interacting with Mitofusin 1 (Mfn1); Tom22 deletion reduces mitochondrial fusion and ATP production in endothelial cells, and overexpression rescues mitochondrial dynamics disrupted by high glucose. Co-immunoprecipitation of Tom22 and Mfn1, siRNA knockdown, overexpression, mitochondrial morphology imaging, ATP measurement Oxidative medicine and cellular longevity Low 31236191
2024 Tom22 stimulates Bax membrane insertion in a cell-free nanodisc system: Tom22 recognizes the hydrophobic GALLL motif in Bax helix α1, triggers conformational changes leading to extrusion and membrane insertion of the C-terminal helix α9; this is required for both constitutive and BH3-activator-stimulated Bax insertion, and the interaction is abolished by D154Y or T174P Bax mutations. Cell-free synthesis in presence of nanodiscs, nanodisc reconstitution, site-directed mutagenesis, liposome permeabilization assay Cell death discovery High 39043635
2025 Molecular dynamics simulations reveal that large motions of Tom22 helices are dynamically coupled to structural rearrangements of the α2 helix within the Tom40 pore; restraining Tom22 helices induces an alternative α2 conformation associated with reduced ion permeability, linking Tom22 receptor dynamics to functional gating of the Tom40 import channel. All-atom molecular dynamics simulations (microsecond timescale) of TOM core complex Journal of chemical information and modeling Low 41172152

Source papers

Stage 0 corpus · 45 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1999 Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase. Nature 253 10519552
1997 Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70. The Journal of biological chemistry 230 9252394
1999 Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. The Journal of biological chemistry 195 10347216
2001 Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small tom proteins, and import receptors. Molecular and cellular biology 145 11259583
2006 TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax. Cell death and differentiation 134 17096026
2007 Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import. The Journal of biological chemistry 131 18063580
1997 The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences. Molecular and cellular biology 115 9343421
2011 In vivo protein-interaction mapping of a mitochondrial translocator protein Tom22 at work. Proceedings of the National Academy of Sciences of the United States of America 105 21896724
2004 Tom22', an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes. Molecular biology and evolution 84 15155803
2013 Glucose-induced regulation of protein import receptor Tom22 by cytosolic and mitochondria-bound kinases. Cell metabolism 80 24093680
2000 Identification and functional analysis of human Tom22 for protein import into mitochondria. Molecular and cellular biology 70 10982837
1996 Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria. Molecular and cellular biology 68 8754801
2019 Porin Associates with Tom22 to Regulate the Mitochondrial Protein Gate Assembly. Molecular cell 58 30738703
2018 In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy. Autophagy 57 29165030
2022 Structural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex receptors. Proceedings of the National Academy of Sciences of the United States of America 52 35733257
2010 Recognition of mitochondrial targeting sequences by the import receptors Tom20 and Tom22. Journal of molecular biology 48 21087612
2003 Mitochondrial import receptors Tom20 and Tom22 have chaperone-like activity. The Journal of biological chemistry 41 14699115
2000 Identification of mammalian TOM22 as a subunit of the preprotein translocase of the mitochondrial outer membrane. The Journal of biological chemistry 36 10900208
1998 An import signal in the cytosolic domain of the Neurospora mitochondrial outer membrane protein TOM22. The Journal of biological chemistry 36 9565567
2017 Mitochondrial inner-membrane protease Yme1 degrades outer-membrane proteins Tom22 and Om45. The Journal of cell biology 34 29138251
1998 Role of the negative charges in the cytosolic domain of TOM22 in the import of precursor proteins into mitochondria. Molecular and cellular biology 33 9584158
2018 Mitochondrial accumulation of amyloid β (Aβ) peptides requires TOMM22 as a main Aβ receptor in yeast. The Journal of biological chemistry 32 29925587
2010 The mitochondrial import gene tomm22 is specifically required for hepatocyte survival and provides a liver regeneration model. Disease models & mechanisms 31 20483998
2004 Targeting and assembly of rat mitochondrial translocase of outer membrane 22 (TOM22) into the TOM complex. The Journal of biological chemistry 30 14985332
2019 Impaired Mitochondrial Fusion and Oxidative Phosphorylation Triggered by High Glucose Is Mediated by Tom22 in Endothelial Cells. Oxidative medicine and cellular longevity 27 31236191
2016 An Outer Mitochondrial Translocase, Tom22, Is Crucial for Inner Mitochondrial Steroidogenic Regulation in Adrenal and Gonadal Tissues. Molecular and cellular biology 23 26787839
2016 The mitochondrial BKCa channel cardiac interactome reveals BKCa association with the mitochondrial import receptor subunit Tom22, and the adenine nucleotide translocator. Mitochondrion 22 27592226
2009 Mitochondrial targeting of cytochrome P450 proteins containing NH2-terminal chimeric signals involves an unusual TOM20/TOM22 bypass mechanism. The Journal of biological chemistry 20 19401463
2000 Genetic analysis of the Drosophila 63F early puff. Characterization of mutations in E63-1 and maggie, a putative Tom22. Genetics 17 10978288
2013 Structural insights into proapoptotic signaling mediated by MTCH2, VDAC2, TOM40 and TOM22. Cellular signalling 16 24269536
2021 A Novel Mitochondrial Complex of Aldosterone Synthase, Steroidogenic Acute Regulatory Protein, and Tom22 Synthesizes Aldosterone in the Rat Heart. The Journal of pharmacology and experimental therapeutics 14 33526603
2011 The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast. FEBS letters 14 22198199
2017 Mitochondrial protein import - Functional analysis of the highly diverged Tom22 orthologue of Trypanosoma brucei. Scientific reports 13 28094338
2020 Depletion of TMEM65 leads to oxidative stress, apoptosis, induction of mitochondrial unfolded protein response, and upregulation of mitochondrial protein import receptor TOMM22. Biochemistry and biophysics reports 9 33319071
2014 Analysis of individual mitochondria via fluorescent immunolabeling with Anti-TOM22 antibodies. Analytical and bioanalytical chemistry 9 24481619
2024 Mitochondrial Translocase TOMM22 Is Overexpressed in Pancreatic Cancer and Promotes Aggressive Growth by Modulating Mitochondrial Protein Import and Function. Molecular cancer research : MCR 8 37878010
2023 TOMM40 and TOMM22 of the Translocase Outer Mitochondrial Membrane Complex rescue statin-impaired mitochondrial dynamics, morphology, and mitophagy in skeletal myotubes. bioRxiv : the preprint server for biology 8 37425714
2023 Korean Red Ginseng-Induced SIRT3 Promotes the Tom22-HIF-1α Circuit in Normoxic Astrocytes. Cells 7 37296633
2017 tomm22 Knockdown-Mediated Hepatocyte Damages Elicit Both the Formation of Hybrid Hepatocytes and Biliary Conversion to Hepatocytes in Zebrafish Larvae. Gene expression 7 28251883
2008 An unusual TOM20/TOM22 bypass mechanism for the mitochondrial targeting of cytochrome P450 proteins containing N-terminal chimeric signals. The Journal of biological chemistry 5 18480056
2024 An introduction to comparative genomics, EukProt, and the reciprocal best hit (RBH) method for bench biologists: Ancestral phosphorylation of Tom22 in eukaryotes as a case study. Methods in enzymology 2 39488375
2024 The membrane insertion of the pro-apoptotic protein Bax is a Tom22-dependent multi-step process: a study in nanodiscs. Cell death discovery 1 39043635
2025 Dynamic Coupling between Tom22 Motions and Tom40 Pore Dynamics Modulates Ion Transport in the Mitochondrial TOM Complex. Journal of chemical information and modeling 0 41172152
2025 Targeting TOMM40 and TOMM22 to Rescue Statin-Impaired Mitochondrial Function, Dynamics, and Mitophagy in Skeletal Myotubes. International journal of molecular sciences 0 41303460
2024 Machine learning and single-cell analysis identify the mitophagy-associated gene TOMM22 as a potential diagnostic biomarker for intervertebral disc degeneration. Heliyon 0 39296040