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Showing TOMM22 — TOM22 is a alias.

TOMM22

Mitochondrial import receptor subunit TOM22 homolog · UniProt Q9NS69

Length
142 aa
Mass
15.5 kDa
Annotated
2026-06-10
48 papers in source corpus 32 papers cited in narrative 31 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TOMM22 (Tom22) is the central organizer and presequence receptor of the mitochondrial outer-membrane TOM translocase, coordinating recognition of incoming preproteins and the architecture of the import channel (PMID:10519552, PMID:9252394). Its cytosolic domain selectively binds presequence-carrying preproteins in a salt-sensitive manner, engaging both the C-terminal part of the presequence and the N-terminal part of the mature protein, and it docks the peripheral receptors Tom20 and Tom70; loss of Tom22 dissociates the translocase into core complexes and abolishes tight channel gating (PMID:10519552, PMID:9252394, PMID:10347216, PMID:10982837). Cryo-EM shows the cytosolic domain forms a three-helix bundle shared with Tom20, with helix H1 critical for presequence binding (PMID:35733257). The single transmembrane domain stabilizes interactions among core TOM subcomplexes, while Tom40 and Tom22 together form a stable channel-active core (GIP) unit (PMID:10519552, PMID:11259583). Tom22 acts along the same recognition pathway as Tom20 and then hands substrates across the membrane: its intermembrane-space (IMS) domain serves as a trans binding site that transfers preproteins to Tim50 of the TIM23 complex (PMID:9343421, PMID:18063580, PMID:21896724). Import efficiency is tuned by phosphorylation — CK2 phosphorylates the precursor at Ser44/Ser46 to promote import, CK1 phosphorylates Thr57 to stimulate assembly with Tom20, and PKA phosphorylates Thr76 to impair import — and in mammalian skeletal muscle CK2 (CSNK2)-dependent phosphorylation of TOMM22 governs its precursor-binding affinity and thereby PINK1-driven mitophagy (PMID:24093680, PMID:29165030). Tom22 levels are controlled by turnover through the inner-membrane Yme1 AAA protease via Mgr1/Mgr3 adaptors that recognize its IMS domain, and by the porin Por1, which sequesters Tom22 to modulate trimeric versus dimeric TOM assembly (PMID:30738703, PMID:29138251). Beyond canonical import, Tom22 functions as a mitochondrial receptor for pro-apoptotic Bax, recognizing the GALLL motif in Bax helix α1 and triggering conformational changes that drive Bax membrane insertion and pore formation (PMID:17096026, PMID:39043635), and it participates in steroidogenesis through a complex with 3βHSD2 (PMID:26787839).

Mechanistic history

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

    Established that Tom22 is a bona fide presequence receptor distinct from Tom20 and Tom70, defining its molecular role in substrate recognition.

    Evidence In vitro binding of purified cytosolic receptor domains to mitochondrial preproteins with presequence-peptide competition

    PMID:9252394

    Open questions at the time
    • Did not resolve which presequence residues are bound
    • Did not address membrane-embedded receptor behavior
  2. 1997 High

    Showed that the IMS domain of Tom22 provides a trans binding site for incoming preproteins, extending its receptor role across the outer membrane.

    Evidence Import assays with yeast mitochondria lacking the Tom22 IMS domain and two-step import protocols

    PMID:9343421

    Open questions at the time
    • Did not identify the downstream acceptor of the IMS domain
    • Essentiality only manifest when cytosolic domains removed
  3. 1999 High

    Defined Tom22 as the structural organizer of the TOM complex, linking its transmembrane domain to complex integrity and channel gating and its cytosolic domain to Tom20/Tom70 docking.

    Evidence Genetic deletion in yeast with biochemical assembly and channel-gating analysis

    PMID:10519552

    Open questions at the time
    • No structural basis for gating control
    • Did not map the docking interfaces with Tom20/Tom70
  4. 1999 High

    Mapped the cytosolic-domain binding site to the C-terminal presequence and N-terminal mature segments, distinguishing presequence from non-cleavable carrier substrates.

    Evidence Peptide-scan binding of purified cytosolic domain to CoxIV and phosphate carrier-derived peptides

    PMID:10347216

    Open questions at the time
    • Peptide-array binding may not reflect folded-substrate geometry
    • Did not test recognition in intact complex
  5. 2000 High

    Demonstrated functional conservation by showing human TOM22 complements yeast Δtom22 and retains domain-specific receptor and Tom20-interaction functions.

    Evidence Immunoprecipitation, deletion-mutant import assays, and yeast complementation

    PMID:10900208 PMID:10982837

    Open questions at the time
    • Mammalian-specific regulation not addressed
    • No structure of human domains at this stage
  6. 2001 High

    Resolved the Tom40-Tom22 GIP core as a stable, channel-active unit that retains preproteins, clarifying the architecture beneath receptor function.

    Evidence Blue native PAGE, denaturant resistance assays, and electrophysiology of purified GIP complex

    PMID:11259583

    Open questions at the time
    • Did not define Tom22 conformational contribution to gating
    • Retention mechanism not molecularly resolved
  7. 2007 High

    Placed Tom20 and Tom22 on the same targeting-signal recognition pathway, ordering the receptor handoff step.

    Evidence In organello TEV cleavage of receptor domains with import of diverse substrates

    PMID:18063580

    Open questions at the time
    • Sequential versus simultaneous action not fully distinguished
    • Substrate-specific differences not exhaustively mapped
  8. 2011 High

    Resolved the substrate trajectory at residue resolution, showing the cytosolic domain accepts precursors and the IMS domain transfers them to Tim50/TIM23.

    Evidence In vivo and in organello site-specific photocrosslinking with substrate/presequence perturbation

    PMID:21896724

    Open questions at the time
    • Kinetics of the handoff unresolved
    • Conformational coupling between domains not defined
  9. 2013 High

    Revealed that import and assembly of Tom22 itself are regulated by opposing kinases (CK2, CK1, PKA), connecting metabolic signaling to TOM biogenesis.

    Evidence In vitro kinase assays, MS site mapping, and import assays with phosphomimetic mutants in yeast

    PMID:24093680

    Open questions at the time
    • Phosphatases reversing these marks not identified
    • In vivo dynamics of switching not quantified
  10. 2017 High

    Identified the turnover route for Tom22 via the Yme1 AAA protease using Mgr1/Mgr3 to recognize its IMS domain, establishing regulated degradation of the receptor.

    Evidence Immunoprecipitation and site-specific photocrosslinking with ATPase-mutant Yme1

    PMID:29138251

    Open questions at the time
    • Physiological triggers of Tom22 degradation unclear
    • Dislocation mechanism of cytosolic domain not fully resolved
  11. 2019 High

    Showed Por1 sequesters Tom22 to tune trimeric versus dimeric TOM assembly and cell-cycle-dependent import preferences, adding a dynamic regulatory layer.

    Evidence Reciprocal Co-IP, BN-PAGE, and cell-cycle synchronization in yeast

    PMID:30738703

    Open questions at the time
    • Mechanism of cell-cycle coupling not defined
    • Mammalian conservation untested here
  12. 2022 High

    Provided the structural basis of Tom22 function, showing a Tom20-like three-helix bundle with helix H1 driving presequence binding.

    Evidence Cryo-EM of human TOM core and TOM-Tom22/Tom20 complexes with structure-guided mutagenesis

    PMID:35733257

    Open questions at the time
    • Dynamic substrate-bound states not captured
    • Full receptor handoff geometry to TIM23 not resolved
  13. 2018 High

    Connected CK2 phosphorylation of mammalian TOMM22 to mitophagy control in skeletal muscle, linking the regulatory switch to PINK1-driven quality control.

    Evidence Muscle-specific Csnk2b KO mouse, in vitro phosphorylation, phosphomimetic rescue, and OCR measurements

    PMID:29165030

    Open questions at the time
    • Mechanism linking precursor-binding affinity to PINK1 accumulation not fully resolved
    • Tissue specificity of the switch unexplored
  14. 2024 Medium

    Reconstituted Tom22's pro-apoptotic receptor function, showing it recognizes the Bax GALLL motif and drives Bax conformational change, insertion, and pore formation.

    Evidence Cell-free nanodisc synthesis, liposome permeabilization, and Bax mutagenesis

    PMID:17096026 PMID:22198199 PMID:39043635

    Open questions at the time
    • In vivo relevance to apoptotic threshold not established
    • Relationship to canonical import function unclear
  15. 2024 Medium

    Extended Tom22 function to disease-relevant import capacity, showing TOMM22 levels set mitochondrial respiratory protein import and are stabilized against ubiquitin-dependent degradation by partner proteins.

    Evidence TOMM22 KD/OE with import and Seahorse assays in cancer cells; Co-IP and ubiquitination/rescue assays with BTN3A3

    PMID:37878010 PMID:42069175

    Open questions at the time
    • E3 ligase mediating TOMM22 ubiquitination not identified
    • Direct versus indirect respiratory effects not separated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How Tom22's multiple non-import roles (Bax activation, steroidogenesis, mitochondrial fusion, Aβ reception) are integrated with, or partitioned from, its core translocase function within a single receptor remains unresolved.
  • No unified structural model spanning import and apoptotic functions
  • Physiological conditions selecting each role undefined
  • Mammalian regulation of moonlighting functions largely uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 5 GO:0038024 cargo receptor activity 4 GO:0060090 molecular adaptor activity 3 GO:0044183 protein folding chaperone 1
Localization
GO:0005739 mitochondrion 4
Pathway
R-HSA-392499 Metabolism of proteins 4 R-HSA-9609507 Protein localization 4 R-HSA-1852241 Organelle biogenesis and maintenance 2 R-HSA-5357801 Programmed Cell Death 2 R-HSA-9612973 Autophagy 1
Partners
BAXMFN1POR1TIM50TOMM20TOMM40TOMM70YME1
Complex memberships
TOM complexTOM core / GIP complex (Tom40-Tom22)

Evidence

Reading pass · 31 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 subcomplexes, while its cytosolic domain serves as a docking point for peripheral receptors Tom20 and Tom70. In the absence of Tom22, the translocase dissociates into core complexes and loses tight channel gating control. Genetic deletion of Tom22 in yeast combined with biochemical analysis of TOM complex assembly and channel gating Nature High 10519552
1997 The purified cytosolic domain of Tom22 selectively recognizes presequence-carrying preproteins in a salt-sensitive manner, functioning as a presequence receptor distinct from Tom20 and Tom70. In vitro binding assays with purified recombinant cytosolic domains of Tom20, Tom22, and Tom70 against mitochondrial preproteins; competition with synthetic presequence peptides The Journal of biological chemistry High 9252394
1999 Tom22 cytosolic domain binds to segments corresponding to the carboxyl-terminal part of the presequence and the amino-terminal part of the mature protein of presequence-carrying preproteins (CoxIV), but does not efficiently bind multiple segments of the non-cleavable phosphate carrier. Binding of purified cytosolic receptor domains to cellulose-bound peptide scans (13-mer peptide libraries) derived from CoxIV and phosphate carrier The Journal of biological chemistry High 10347216
1997 The intermembrane space (IMS) domain of Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences during outer membrane translocation, consistent with the acid chain hypothesis; this function becomes essential when cytosolic receptor domains are removed or during two-step import. Import assays using yeast mutant mitochondria lacking the IMS domain of Tom22; two-step import protocol (accumulation without ΔΨ then import after ΔΨ restoration); removal of cytosolic receptor domains Molecular and cellular biology High 9343421
2001 Tom40 and Tom22 form a highly stable core unit (GIP complex) that retains accumulated preproteins and exhibits characteristic TOM channel activity with two coupled conductance states; the GIP complex is resistant to urea and alkaline pH, and preprotein retention is not dependent on ionic interactions. Blue native PAGE, urea/salt/detergent treatment of isolated TOM complexes, electrophysiology of purified GIP complex from outer membrane vesicles Molecular and cellular biology High 11259583
2006 TOM22 functions as a mitochondrial receptor for the pro-apoptotic protein Bax; the interaction involves the first alpha helix of Bax and two central alpha helices. Knockdown of TOM22 inhibits Bax association with mitochondria and prevents Bax-dependent apoptosis. Bacterial two-hybrid assay, crosslinking strategies, peptide mapping, antisense knockdown of TOM22, yeast haploid strain with reduced TOM22 Cell death and differentiation High 17096026
2007 Tom20 and Tom22 are involved in the same step or sequential steps along the same pathway for targeting signal recognition during mitochondrial protein import; deletion of their receptor domains has similar effects across diverse import substrates. In vitro cleavage of receptor domains via introduced TEV protease sites in yeast; import assays of multiple mitochondrial precursor proteins The Journal of biological chemistry High 18063580
2011 The cytosolic receptor domain of Tom22 accepts substrate precursor proteins, and the IMS domain of Tom22 transfers them to Tim50 of the inner-membrane translocator TIM23 complex, as mapped at single amino acid residue resolution in vivo. In vivo and in organello site-specific photocrosslinking; changes in crosslinking patterns induced by excess substrate or presequence peptides Proceedings of the National Academy of Sciences of the United States of America High 21896724
2013 CK2 constitutively phosphorylates the cytosolic precursor of Tom22 at Ser44 and Ser46, promoting its import into the TOM complex. CK1 (bound to mitochondria) phosphorylates Tom22 at Thr57 and stimulates assembly of Tom22 and Tom20. PKA phosphorylates the precursor of Tom22 at Thr76 and impairs its import, acting oppositely to CK1 and CK2. In vitro kinase assays, phosphorylation site mapping by mass spectrometry, import assays with phosphomimetic/phospho-null mutants, glucose-stimulated signaling experiments in yeast Cell metabolism High 24093680
2000 Human TOM22 (hTom22) forms a complex with Tom20, functions as an import receptor via its cytosolic domain, and complements Δtom22 yeast cells; the C-terminal segment of the cytosolic domain is important for presequence binding, the N-terminal domain binds the mature portion of preproteins, and an internal segment of the cytosolic domain mediates interaction with Tom20. Immunoprecipitation, import inhibition assay with deletion mutants, cell-free binding studies, complementation of yeast Δtom22 Molecular and cellular biology High 10982837
2000 Mammalian TOM22 (1C9-2) is stably associated with TOM40 in an ~400 kDa complex at the mitochondrial outer membrane and functionally complements Δtom22 yeast cells for growth and mitochondrial protein import. Immunopurification, blue native PAGE, import inhibition with antibodies, complementation of yeast Δtom22 The Journal of biological chemistry High 10900208
2022 Cryo-EM structure of human TOM core complex at 2.53 Å, and TOM complex with Tom22 and Tom20 cytosolic domains at 3.74 Å, reveals that Tom20 and Tom22 share a similar three-helix bundle structural feature in their cytosolic domains. Structure-guided mutagenesis shows the Tom22 cytosolic domain is responsible for presequence binding, with helix H1 being critical. Cryo-EM structure determination, structure-guided mutagenesis, biochemical binding assays Proceedings of the National Academy of Sciences of the United States of America High 35733257
2018 In mammalian skeletal muscle, CSNK2/CK2-mediated phosphorylation of TOMM22 controls mitophagy: loss of CSNK2 reduces TOMM22 phosphorylation and its binding affinity for mitochondrial precursor proteins, leading to PINK1 accumulation and mitophagy. Phosphomimetic TOMM22 rescues oxygen consumption rate and normalizes mitophagy in Csnk2b-KO muscle. Skeletal muscle-specific Csnk2b conditional knockout mouse, in vitro phosphorylation assays with muscle lysates, electron microscopy for autophagosomes, electroporation of phosphomimetic Tomm22 in vivo, oxygen consumption rate measurement Autophagy High 29165030
2019 Porin (Por1) acts as a sink to bind newly imported Tom22, modulating its integration into the trimeric TOM complex. Por1 sequestration of Tom22 dissociated from the trimeric TOM complex enhances the dimeric TOM complex (lacking Tom22), which is preferable for import of TIM40/MIA-dependent proteins. Por1 also contributes to cell-cycle-dependent variation of the functional trimeric TOM complex. Co-immunoprecipitation, blue native PAGE, genetic analysis, cell-cycle synchronization experiments in yeast Molecular cell High 30738703
1998 A short segment of the cytosolic domain of Neurospora TOM22 contains a novel internal import signal with a net positive charge that is essential for targeting and assembly of TOM22 into the outer membrane; the transmembrane segment and IMS domain alone are insufficient for import. In vitro import studies with TOM22 deletion and charge-reversal mutants in Neurospora The Journal of biological chemistry Medium 9565567
1998 An abundance of negative charges in the cytosolic domain of Neurospora TOM22 is not essential for preprotein binding or import; however, other structural features of this domain are required (deletion of the entire region abolishes function). Systematic charge-neutralization mutagenesis of the cytosolic domain, mitochondrial import assays, precursor binding assays with outer membrane vesicles, complementation in heterokaryon Molecular and cellular biology Medium 9584158
2004 Rat TOM22 targeting to the mitochondrial outer membrane and assembly into the TOM complex requires three structural elements: an acidic alpha-helical cytoplasmic import sequence ~30 residues upstream of the TMD, the TMD with appropriate hydrophobicity, and a 20-residue C-terminal IMS segment. The import sequence interacts intramolecularly with TMD and C-tail, and also with Tom20 by yeast two-hybrid. Systematic deletion/mutation analysis in HeLa cells with confocal microscopy, cell fractionation, blue native PAGE, yeast two-hybrid The Journal of biological chemistry Medium 14985332
2003 The cytosolic domain of Tom22 has chaperone-like activity, preventing substrate proteins (e.g., citrate synthase) from aggregating. This activity is inhibited by presequence peptide, suggesting the presequence binding site and the chaperone active site are identical or overlapping. In vitro aggregation suppression assays with purified cytosolic domains of Tom20 and Tom22; competition with presequence peptide The Journal of biological chemistry Medium 14699115
2010 NMR studies of plant ScTom22 show it binds presequences; AtTom22 (plant) does not bind presequences but instead binds to the AtTom20 receptor at the same site as presequences, suggesting it competes with presequences to enable their progression along the import pathway. NMR spectroscopy of cytosolic domains of AtTom20, AtTom22, and ScTom22 with presequence peptides Journal of molecular biology Medium 21087612
2017 Mitochondrial inner-membrane AAA protease Yme1 degrades outer-membrane Tom22 via its adaptor proteins Mgr1 and Mgr3, which recognize the IMS domain of Tom22; the ATPase activity of Yme1 can dislocate the cytoplasmic domain of substrates into the IMS for proteolysis. Immunoprecipitation, in vivo site-specific photocrosslinking to map Mgr1/Mgr3 interactions with Tom22 IMS domain, ATPase-mutant Yme1 analysis The Journal of cell biology High 29138251
2018 TOMM22 is the main mitochondrial receptor for amyloid-β (Aβ) peptides in yeast mitochondria; residues 25-42 of Aβ mediate the specific interaction with TOMM22. Aβ is then proposed to be transferred to TOMM40 and transported through the TOM channel. Yeast genetics (tom22 deletion), direct binding assays with Aβ peptide fragments, mitochondrial import assays The Journal of biological chemistry Medium 29925587
2016 Tom22 is essential for steroidogenesis: Tom22 knockdown abolishes progesterone conversion in steroidogenic cells, and Tom22 forms a ~500 kDa complex with 3βHSD2 at the mitochondrial outer membrane. The IMS C-terminal segment of Tom22 interacts with a specific region of 3βHSD2. Tom22 absence inhibits 3βHSD2 expression but not import of CYP450scc or aldosterone synthase. siRNA knockdown, blue native PAGE, electron microscopy for localization, co-immunoprecipitation, steroidogenesis functional assays in MA-10 and NCI cells Molecular and cellular biology Medium 26787839
2021 Tom22, aldosterone synthase (P450c11AS), and intramitochondrial 30-kDa StAR form a 110-kDa trimolecular complex required for aldosterone synthesis in the rat heart, as demonstrated by protein crosslinking and co-immunoprecipitation. Blue native PAGE, immunoblotting, protein crosslinking, co-immunoprecipitation, mass spectrometry The Journal of pharmacology and experimental therapeutics Medium 33526603
2011 Human Tom22 cytosolic domain expression in yeast increases Bax mitochondrial localization but decreases the proportion of active Bax and interferes with Bax oligomerization, suggesting the cytosolic domain of Tom22 promotes a membrane-competent but non-oligomeric Bax conformation. Co-immunoprecipitation, blue native PAGE, yeast expression system with human Bax FEBS letters Medium 22198199
2024 Tom22 stimulates Bax membrane insertion in a cell-free nanodisc system: Tom22 recognizes the GALLL hydrophobic motif in Bax helix α1, triggering conformational changes that lead to extrusion and membrane insertion of the C-terminal hydrophobic Hα9. Tom22-activated Bax forms ~5-nm pores in nanodiscs. D154Y and T174P mutations in Bax impair this Tom22-dependent mechanism. Cell-free synthesis with nanodiscs, liposome permeabilization assay, mutagenesis of Bax Cell death discovery Medium 39043635
2025 Molecular dynamics simulations reveal that Tom22 helices undergo large motions coupled to global structural rearrangements in the TOM complex, particularly with the α2 helix within the Tom40 pore, and restraining Tom22 helices reduces ion permeability, linking Tom22 receptor dynamics to pore gating. All-atom molecular dynamics simulations (microsecond-scale) with and without restraints on Tom22 helices; ion permeability measurements in silico Journal of chemical information and modeling Low 41172152
2019 Tom22 interacts with Mfn1 and modulates mitochondrial fusion: Tom22 deletion reduces mitochondrial fusion, ATP production, and increases apoptosis in endothelial cells; Tom22 overexpression restores mitochondrial dynamics and OXPHOS impaired by high glucose. Co-immunoprecipitation, siRNA knockdown, overexpression in HUVECs, mitochondrial morphology imaging, ATP measurement Oxidative medicine and cellular longevity Medium 31236191
2016 Mitochondrial BKCa channel interacts with Tom22 via its transmembrane domain, and the BKCa 50-amino-acid DEC splice insert facilitates interaction with ANT but not Tom22. BKCa and Tom22 co-immunoprecipitate and co-segregate into mitochondrial fractions. Directed proteomics, co-immunoprecipitation, cell fractionation in HEK293T cells Mitochondrion Low 27592226
2009 Certain cytochrome P450 proteins with chimeric mitochondrial targeting signals (CYP+33/1A1, CYP2B1) can bypass TOM20, TOM22, and TOM70 for translocation through TOM40, while others (CYP+5/1A1, CYP2E1) bypass TOM20 and TOM22 but require TOM70. This bypass occurs when CYP proteins interact sequentially with both Hsp70 and Hsp90. Antibody inhibition of specific TOM subunits, import assays, co-immunoprecipitation with chaperones The Journal of biological chemistry Medium 18480056 19401463
2024 TOMM22 overexpression in pancreatic cancer cells increases import of mitochondrial proteins associated with respiration, RCI activity, NAD+/NADH ratio, oxygen consumption rate, membrane potential, and ATP production. TOMM22 silencing decreases these and suppresses malignant growth, placing TOMM22 upstream of mitochondrial respiratory function. TOMM22 siRNA knockdown and overexpression in pancreatic cancer cell lines, mitochondrial protein import assays, RCI activity measurement, Seahorse metabolic analysis Molecular cancer research : MCR Medium 37878010
2026 BTN3A3 interacts with TOMM22 at mitochondria (identified by mass spectrometry and Co-IP); sorafenib stress promotes BTN3A3 mitochondrial translocation where it shields TOMM22 from ubiquitin-proteasome-dependent degradation. BTN3A3 deficiency leads to TOMM22 depletion, mitochondrial fragmentation, and impaired OXPHOS. Mass spectrometry, co-immunoprecipitation, ubiquitination assays, TOMM22 knockdown/rescue, live-cell imaging of BTN3A3 translocation, in vivo xenograft Cancer letters Medium 42069175

Source papers

Stage 0 corpus · 48 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1999 Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase. Nature 255 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 197 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 147 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 135 17096026
2007 Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import. The Journal of biological chemistry 133 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 116 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 106 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 82 24093680
2000 Identification and functional analysis of human Tom22 for protein import into mitochondria. Molecular and cellular biology 71 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 61 30738703
2018 In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy. Autophagy 59 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 56 35733257
2010 Recognition of mitochondrial targeting sequences by the import receptors Tom20 and Tom22. Journal of molecular biology 50 21087612
2003 Mitochondrial import receptors Tom20 and Tom22 have chaperone-like activity. The Journal of biological chemistry 42 14699115
2017 Mitochondrial inner-membrane protease Yme1 degrades outer-membrane proteins Tom22 and Om45. The Journal of cell biology 36 29138251
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
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 28 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 21 19401463
2013 Structural insights into proapoptotic signaling mediated by MTCH2, VDAC2, TOM40 and TOM22. Cellular signalling 17 24269536
2000 Genetic analysis of the Drosophila 63F early puff. Characterization of mutations in E63-1 and maggie, a putative Tom22. Genetics 17 10978288
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
2024 Mitochondrial Translocase TOMM22 Is Overexpressed in Pancreatic Cancer and Promotes Aggressive Growth by Modulating Mitochondrial Protein Import and Function. Molecular cancer research : MCR 11 37878010
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
2023 Korean Red Ginseng-Induced SIRT3 Promotes the Tom22-HIF-1α Circuit in Normoxic Astrocytes. Cells 8 37296633
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
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
2025 Targeting TOMM40 and TOMM22 to Rescue Statin-Impaired Mitochondrial Function, Dynamics, and Mitophagy in Skeletal Myotubes. International journal of molecular sciences 1 41303460
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
2026 Thioredoxin protects against diabetic hearing loss by regulating TOMM22 mediated mitochondrial autophagy in hair cells and inhibiting microglial M1 polarization. Scientific reports 0 41862549
2026 The BTN3A3-TOMM22 axis preserves mitochondrial homeostasis to facilitate HCC stemness and drug resistance. Cancer letters 0 42069175
2026 Pan-cancer multi-omics analysis identifies TOMM22 as an oncogenic driver and therapeutic target in LIHC via ferroptosis regulation. Naunyn-Schmiedeberg's archives of pharmacology 0 42101633
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
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

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