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The protein encoded by this gene is named for its structural resemblance to the members of the mitochondrial carrier protein family.[5][7] The MTCH1 gene contains 12 exons and produces four isoforms. These isoforms arise from alternative splicing of exon 8 and two potential start codons, which results in the deletion of 17 amino acid residues in the hydrophilic loop between two transmembrane domains of some isoforms.[9][10] Though they differ in sequence and length, the four isoforms still share a similar topological structure, including six transmembrane domains, one of which is responsible for localization to the outer mitochondrial membrane (OMM), and two N-terminal apoptotic domains. As a result, all four isoforms retain these apoptotic domains and mitochondrial localization, both of which are required for the protein's proapoptotic function.[7][9][10]
MTCH1 is a proapoptotic protein that localizes to the OMM and induces apoptosis independently of BAX and BAK.[6][7] One possible mechanism proposes that its interactions with the mitochondrial permeability transition pore (MPTP) complex leads to depolarization of the mitochondrial membrane, release of cytochrome C, and activation of caspase-3.[5][7] Expression of this protein is observed in 16 different tissue types, indicating that the protein may serve a housekeeping function.[10]
123456Lamarca, V; Marzo, I; Sanz-Clemente, A; Carrodeguas, JA (May 2008). "Exposure of any of two proapoptotic domains of presenilin 1-associated protein/mitochondrial carrier homolog 1 on the surface of mitochondria is sufficient for induction of apoptosis in a Bax/Bak-independent manner". European Journal of Cell Biology. 87 (5): 325–34. doi:10.1016/j.ejcb.2008.02.004. PMID18375015.
123Vural, B; Sehitoğlu, E; Cavuş, F; Yalçınkaya, N; Haytural, H; Küçükerden, M; Ulusoy, C; Uğurel, E; Turan, S; Bulut, L; Türkoğlu, R; Shugaiv, E; Kürtüncü, M; Atakan, S; Güre, AO; Gül, A; Eraksoy, M; Akman-Demir, G; Tüzün, E (15 October 2013). "Mitochondrial carrier homolog 1 (Mtch1) antibodies in neuro-Behçet's disease". Journal of Neuroimmunology. 263 (1–2): 139–44. doi:10.1016/j.jneuroim.2013.08.007. hdl:11693/12552. PMID24035008. S2CID13300599.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Lamarca V, Sanz-Clemente A, Pérez-Pé R, etal. (2007). "Two isoforms of PSAP/MTCH1 share two proapoptotic domains and multiple internal signals for import into the mitochondrial outer membrane". Am. J. Physiol., Cell Physiol. 293 (4): C1347–C1361. doi:10.1152/ajpcell.00431.2006. PMID17670888. S2CID43241603.
