IMMT

Not to be confused with Institute of Minerals and Materials Technology.

IMMT
Identifiers
Aliases	IMMT, HMP, MINOS2, P87, P87/89, P89, PIG52, Mic60, PIG4, inner membrane mitochondrial protein, MICOS60, mitofilin
External IDs	OMIM: 600378 MGI: 1923864 HomoloGene: 38234 GeneCards: IMMT
Gene location (Human) Chr. Chromosome 2 (human) Band 2p11.2|2 Start 86,143,932 bp End 86,195,472 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 C1 Start 71,808,315 bp End 71,854,372 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left ventricle gastrocnemius muscle biceps brachii right ventricle body of tongue deltoid muscle triceps brachii muscle left adrenal gland renal medulla rectum Top expressed in myocardium of ventricle right ventricle cardiac muscles soleus muscle digastric muscle brown adipose tissue extraocular muscle tibialis anterior muscle sternocleidomastoid muscle atrium More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding RNA binding Cellular component integral component of membrane mitochondrial inner membrane myelin sheath MICOS complex membrane mitochondrion Biological process cristae formation mitochondrial calcium ion homeostasis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10989 76614 Ensembl ENSG00000132305 ENSMUSG00000052337 UniProt Q16891 Q8CAQ8 RefSeq (mRNA) NM_001100169 NM_001100170 NM_006839 NM_001253681 NM_001253686 NM_001253687 NM_001253688 NM_001253689 NM_029673 NM_001362134 NM_001362136 NM_001362137 NM_001362138 RefSeq (protein) NP_001093639 NP_001093640 NP_006830 NP_001240610 NP_001240615 NP_001240616 NP_001240617 NP_001240618 NP_083949 NP_001349063 NP_001349065 NP_001349066 NP_001349067 Location (UCSC) Chr 2: 86.14 – 86.2 Mb Chr 6: 71.81 – 71.85 Mb PubMed search
Wikidata
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Mitochondrial inner membrane protein is a protein that in humans is encoded by the IMMT gene.)

IMMT encodes an inner mitochondrial membrane (IMM) protein in the nucleus. It is posttranslational transported to the IMM. Mic60/Mitofilin (encoded by the IMMT gene) is a core subunit of the MICOS-complex, directly located next to cristae junctions (CJ). Human Mic60 exists in two isoforms of different size, anchored to the IMM via its N-terminus, while most of the protein is located to the inner mitochondrial space (IMS).

Function

Mic60 is evolutionary one of the oldest MICOS subunits as homologous were found in anaerobic prokaryotes. It is mainly present in two isoforms (ca. 88 and 90 kDa). In the brain, four isoforms are known, which differ in their isoelectric point due to different post-translational modifications. The amino terminus of Mic60 is anchored in the IM, while most of the protein is extended to the IMS. C-terminal Mic60 has a conserved mitofilin domain which is crucial for building the MICOS-complex. A central coiled-coil domain is required to enable protein-protein interactions.

Interactions

Mic60 indirectly interacts with all known MICOS-complex and SAM complex components. It directly interacts with Mic25, Mic19 and SAM50. Together with Mic25 and Mic19, Mic60 forms the Mic60-Mic19-Mic25 subcomplex. This subcomplex, especially Mic60, is crucial for the physical contact between the IMM and the outer mitochondrial membrane (OMM) via its interaction with SAM50. Mic60 also interacts with the translocase of the OMM (TOM) and the translocase of the IMM (TIM) to ensure the localization of Mic60 near to CJs. Through its interaction with TOM and TIM, Mic60 additionally influences the import of precursor proteins.

Localisation/Import

Mic60 is translated in the cytosol and translocated into the IMS via TOMM40. TIMM23 transports Mic60 into the IM, where a mitochondrial processing peptidase (MPP) cleaves of the N-terminal mitochondrial targeting signal (MTS). Mic60 is anchored in the IMM through its transmembrane (TM) domain.

Interactions

IMMT has been shown to interact with BAT2.)

Further reading

• Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–320. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• Maruyama K, Sugano S (January 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. PMID 8125298.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, et al. (September 1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Research. 6 (9): 807–828. doi:10.1101/gr.6.9.807. PMID 8889549.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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. PMID 9373149.
• Liu J, Akoulitchev S, Weber A, Ge H, Chuikov S, Libutti D, et al. (February 2001). "Defective interplay of activators and repressors with TFIH in xeroderma pigmentosum". Cell. 104 (3): 353–363. doi:10.1016/S0092-8674(01)00223-9. PMID 11239393. S2CID 16066683.
• Bernert G, Fountoulakis M, Lubec G (December 2002). "Manifold decreased protein levels of matrin 3, reduced motor protein HMP and hlark in fetal Down's syndrome brain". Proteomics. 2 (12): 1752–1757. doi:10.1002/1615-9861(200212)2:12<1752::AID-PROT1752>3.0.CO;2-Y. PMID 12469345. S2CID 32160196.
• Millar JK, Christie S, Porteous DJ (November 2003). "Yeast two-hybrid screens implicate DISC1 in brain development and function". Biochemical and Biophysical Research Communications. 311 (4): 1019–1025. doi:10.1016/j.bbrc.2003.10.101. PMID 14623284.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (January 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–167. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Goehler H, Lalowski M, Stelzl U, Waelter S, Stroedicke M, Worm U, et al. (September 2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Molecular Cell. 15 (6): 853–865. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
• John GB, Shang Y, Li L, Renken C, Mannella CA, Selker JM, et al. (March 2005). "The mitochondrial inner membrane protein mitofilin controls cristae morphology". Molecular Biology of the Cell. 16 (3): 1543–1554. doi:10.1091/mbc.E04-08-0697. PMC 551514. PMID 15647377.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, et al. (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–968. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, et al. (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–814. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
• Camargo LM, Collura V, Rain JC, Mizuguchi K, Hermjakob H, Kerrien S, et al. (January 2007). "Disrupted in Schizophrenia 1 Interactome: evidence for the close connectivity of risk genes and a potential synaptic basis for schizophrenia". Molecular Psychiatry. 12 (1): 74–86. doi:10.1038/sj.mp.4001880. PMID 17043677.
• Xie J, Marusich MF, Souda P, Whitelegge J, Capaldi RA (July 2007). "The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC11". FEBS Letters. 581 (18): 3545–3549. doi:10.1016/j.febslet.2007.06.052. PMID 17624330. S2CID 726629.