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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

TOM22 Tom22p

Tom22, MOM22
The protein encoded by this gene is an integral membrane protein of the mitochondrial outer membrane. The encoded protein interacts with TOMM20 and TOMM40, and forms a complex with several other proteins to import cytosolic preproteins into the mitochondrion. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Tom20, Tom40, CAN, ACID, STEP
Papers on Tom22
A comparison of mitochondrial DNA isolation methods in frozen post-mortem human brain tissue--applications for studies of mitochondrial genetics in brain disorders.
Lunnon et al., London, United Kingdom. In Biotechniques, Oct 2015
Our data show that a commercial method from Miltenyi Biotec, which magnetically isolates mitochondria using antibodies raised against the mitochondrial import receptor subunit TOM22, gives significant mtDNA enrichment and should be considered the method of choice for mtDNA studies in frozen brain tissue.
Structural insights into proapoptotic signaling mediated by MTCH2, VDAC2, TOM40 and TOM22.
Davidovskii et al., Minsk, Belarus. In Cell Signal, 2014
Shortly thereafter, several MOM proteins, such as VDAC2, MTCH2, TOM22 and TOM40, have been identified as the Bax, Bak and tBid receptors that are indispensable in MOMP, but the underlying mechanisms are elusive.
Analysis of individual mitochondria via fluorescent immunolabeling with Anti-TOM22 antibodies.
Arriaga et al., Minneapolis, United States. In Anal Bioanal Chem, 2014
Mitochondria were fluorescently labeled with DsRed2, while antibodies targeting the TOM22 protein, one of nine proteins comprising the TOM complex, were conjugated to the Atto-488 fluorophore.
Unique components of the plant mitochondrial protein import apparatus.
Whelan et al., Crawley, United Kingdom. In Biochim Biophys Acta, 2013
This includes the evolution of two unique outer membrane import receptors, plant Translocase of outer membrane 20 kDa subunit (TOM20) and Outer membrane protein of 64 kDa (OM64), the loss of a receptor domain from an ancestral import component, Translocase of outer membrane 22 kDa subunit (TOM22), evolution of unique features in the disulfide relay system of the inter membrane space, and the addition of an extra membrane spanning domain to another ancestral component of the inner membrane, Translocase of inner membrane 17 kDa subunit (TIM17).
Efficient isolation of pure and functional mitochondria from mouse tissues using automated tissue disruption and enrichment with anti-TOM22 magnetic beads.
de Angelis et al., München, Germany. In Plos One, 2012
To fulfill the need of a reproducible isolation method from solid tissues, which is suitable to handle parallel samples simultaneously, we developed a protocol based on anti-TOM22 (translocase of outer mitochondrial membrane 22 homolog) antibody-coupled magnetic beads.
ER stress-mediated apoptosis induced by celastrol in cancer cells and important role of glycogen synthase kinase-3β in the signal network.
Guo et al., Shanghai, China. In Cell Death Dis, 2012
Possible target-related proteins of celastrol such as endoplasmic reticulum protein 29 (ERP29) and mitochondrial import receptor Tom22 (TOM22) were found by 2-DE analysis of total cellular protein expression profiles.
The role of miRNAs and EBV BARTs in NPC.
Raab-Traub et al., Chapel Hill, United States. In Semin Cancer Biol, 2012
Studies indicate that PUMA and TOMM22 as potential targets for miRNA-BART viral transcripts.
A micropreparation of mitochondria from cells using magnetic beads with immunoaffinity.
Liu et al., Beijing, China. In Anal Biochem, 2012
The polyclonal antibodies against the truncated CYB5B and SYNJ2BP exhibited specific recognition to mitochondria and wider sensitivity to several tested mouse tissues and cell lines, whereas the antibody 22-kDa translocase of the outer mitochondrial membrane (TOM22) nearly missed detection of mitochondria in the liver and responded minimally to mitochondria from H9C2 and L-02 cells.
The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast.
Manon et al., Bordeaux, France. In Febs Lett, 2012
The interaction with the cytosolic domain of Tom22 helps Bax to acquire a conformation able to interact with the outer mitochondrial membrane.
Mannheimia haemolytica leukotoxin binds cyclophilin D on bovine neutrophil mitochondria.
Czuprynski et al., Madison, United States. In Microb Pathog, 2011
We demonstrate that LKT binds bovine neutrophil mitochondria and co-immunoprecipitates with TOM22 and TOM40, which are members of the translocase of the outer mitochondrial (TOM) membrane family.
ALS-linked mutant superoxide dismutase 1 (SOD1) alters mitochondrial protein composition and decreases protein import.
Miller et al., Saint Louis, United States. In Proc Natl Acad Sci U S A, 2011
Direct import assays revealed a 30% decrease in protein import only in spinal cord mitochondria, despite an increase in the mitochondrial import components TOM20, TOM22, and TOM40.
Identification and characterization of the mitochondrial targeting sequence and mechanism in human citrate synthase.
Chang et al., Tainan City, Taiwan. In J Cell Biochem, 2009
Moreover, RNA interference (RNAi)-mediated gene silencing of the preprotein import receptors, including TOM20, TOM22, and TOM70, showed that all three preprotein import receptors are required for transporting CSa into the mitochondria.
Mitochondrial targeting of cytochrome P450 proteins containing NH2-terminal chimeric signals involves an unusual TOM20/TOM22 bypass mechanism.
Avadhani et al., Philadelphia, United States. In J Biol Chem, 2009
CYP+33/1A1 and CYP2B1 did not require peripheral TOM70, TOM20, or TOM22 for translocation through the channel-forming TOM40 protein.
Isolation of functional pure mitochondria by superparamagnetic microbeads.
Wiesner et al., Köln, Germany. In Anal Biochem, 2009
The new approach is based on superparamagnetic microbeads conjugated to anti-TOM22 antibody.
Bax inserts into the mitochondrial outer membrane by different mechanisms.
Vallette et al., Nantes, France. In Febs Lett, 2008
We have recently shown that TOM22, a mitochondrial outer membrane receptor, is important for insertion, although other reports have suggested that only mitochondrial lipids are involved in this process.
Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import.
Endo et al., Nagoya, Japan. In J Biol Chem, 2008
beta2GP1-dependent uptake is mediated by bridging of the target cell to the phagocyte through the protein C- and N-terminal domains, respectively
Biogenesis of the mitochondrial TOM complex: Mim1 promotes insertion and assembly of signal-anchored receptors.
Wiedemann et al., Freiburg, Germany. In J Biol Chem, 2008
Data Show that Tom22 are anchored in the outer membrane by a single transmembrane alpha-helix, located in the C-terminal portion of Tom22 (tail-anchored) and insertion of the precursor of Tom22 into the outer membrane requires pre-existing Tom receptors.
The Tim21 binding domain connects the preprotein translocases of both mitochondrial membranes.
Zeth et al., Martinsried, Germany. In Embo Rep, 2006
We also identified a core sequence of Tom22 that binds to Tim21. Furthermore, negatively charged amino-acid residues of Tom22 are important for binding to Tim21. Here we suggest a mechanism for the TOM-TIM interaction.
The mitochondrial receptor complex: a central role of MOM22 in mediating preprotein transfer from receptors to the general insertion pore.
Neupert et al., München, Germany. In Cell, 1993
Here we report on the structure and function of MOM22.
Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins.
Neupert et al., München, Germany. In Nature, 1991
The mitochondrial import receptors MOM19 and MOM72 form a complex with two other proteins of the mitochondrial outer membrane, MOM38 and MOM22.
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