MTA1

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This article is about proteins. For the Islamic TV channel, see MTA 1.
MTA1
Protein MTA1 PDB 2crg.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases MTA1
External IDs MGI: 2150037 HomoloGene: 3442 GeneCards: 9112
RNA expression pattern
PBB GE MTA1 202247 s at tn.png

PBB GE MTA1 211783 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001203258
NM_004689

NM_054081

RefSeq (protein)

NP_001190187.1
NP_004680.2

XP_006515485.1
XP_006536382.1

Location (UCSC) Chr 14: 105.42 – 105.47 Mb Chr 12: 113.1 – 113.14 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Metastasis-associated protein MTA1 is a protein that in humans is encoded by the MTA1 gene. MTA1 is the founding member of the MTA family of genes.[1][2] MTA1 is primarily localized in the nucleus but also found to be distributed in the extra-nuclear compartments.[3][4] MTA1 is a component of several chromatin remodeling complexes including the nucleosome remodeling and deacetylation complex (NuRD).[5][6] MTA1 regulates gene expression by functioning as a coregulator to integrate DNA-interacting factors to gene activity.[7] MTA1 participates in physiological functions in the normal and cancer cells.[8][9] MTA1 is one of the most upregulated proteins in human cancer and associates with cancer progression, aggressive phenotypes, and poor prognosis of cancer patients.[10][6]

Discovery[edit]

MTA1 was first cloned by Toh, Pencil and Nicholson in 1994 as a differentially expressed gene in a highly metastatic rat breast cancer cell line.[1][2] The role in MTA1 in chromatin remodeling was deduced due to the presence of MTA1 polypeptides in the NuRD complex.[5] The first direct target of the MTA1-NuRD complex was ERα.[11]

Gene and spliced variants[edit]

The MTA1 is 715/703 amino acids long, coded by one of three genes of the MTA family and localized on chromosome 14q32 in human and on chromosome 12F in mouse. There are 21 exons spread over a region of about 51-kb in human MTA1. Alternative splicing from 21 exons generates 20 transcripts, ranging from 416-bp to 2.9-kb long.[12] However, open-reading frames are present only in eight spliced transcripts which code six proteins and two polypeptides and remaining transcripts are non-coding long RNAs some of which retain intron sequences. Murine Mta1 contains three protein coding transcripts and three non-coding RNA transcripts.[12] Among human MTA1 variants, only two spliced variants are characterized: ZG29p variant is derived from the c-terminal MTA1, with 251 amino acids and 29-kDa molecular weight;[13] and MTA1s variant generated from alternative splicing of a middle exon followed by a frame-shift, is 430 amino acids and 47-kDa molecular weight.[14]

Protein domains[edit]

The conserved domains of MTA1 include a BAH (Bromo-Adjacent Homology), a ELM2 (egl-27 and MTA1 homology), a SANT (SWI, ADA2, N-CoR, TFIIIB-B) and a GATA-like zinc finger. The C-terminal divergent region of MTA1 has an Src homology 3-binding domain, acidic regions, and nuclear localization signals. The presence of these domains revealed the role of MTA1 in interactions with modified or unmodified histone and non-histone proteins, chromatin remodeling, and modulation of gene transcription.[6][15][16][17] MTA1 undergoes multiple post-translation modifications: acetylation on lysine 626, ubiquitination on lysine 182 and lysine 626, sumoylation on lysine 509, and methylation on lysine 532.[18][19][20][21] The structural insights of MTA1 domains are deduced from studies involving complexes with HDAC1 or RbAp48 subunits of the NuRD complexes.[15][16] The MTA1s variant is an N-terminal portion of MTA1 without nuclear localization sequence but contains a novel sequence of 33 amino acids in its C-terminal region. The novel sequence harbors a nuclear receptor binding motif LXXLL which confers MTA1 with an ability to interact with estrogen receptor alpha or other type I nuclear receptors.[14] The ZG29p variant represents the c-terminal MTA1 with two proline-rich SH3 binding sites.[13][22]

Regulation[edit]

Expression of MTA1 is influenced by transcription and non-transcriptional mechanisms. MTA1 expression is regulated by growth factors, growth factor receptors, oncogenes, environmental stress, ionizing radiation, inflammation, and hypoxia.[6][9] The transcription of MTA1 is stimulated by transcriptional factors including, c-Myc,[23]SP1,[24] CUTL1 homeodomain,[25] NF-ḵB,[26] HSF1,[27] HIF-1a,[28] and Clock/BMAL1 complex,[29] and inhibited by p53.[30] Non-genomic mechanisms of MTA1 expression include post-transcriptional regulations such as ubiquitination by RING-finger ubiquitin-protein ligase COP1 [31] or interaction with tumor suppressor ARF [24] or micro-RNAs such as miR-30c, miR-661 and miR-125a-3p.[32][33][34][35]

Targets[edit]

Functions of MTA1 are regulated by its post-translational modifications, modulating the roles of effector molecules, interacting with other regulatory proteins and chromatin remodeling machinery, and modulating the expression of target genes via interacting with the components of the NuRD complex including HDACs.[6][15][16]

MTA1 suppresses transcription of breast cancer type 1 susceptibility gene,[36] PTEN, [37]p21WAF,[38]guanine nucleotide-binding protein G(i) subunit alpha-2,[18]SMAD family member 7,[39] nuclear receptor subfamily 4 group A member 1,[40] and homeobox protein SIX3,[41] and represses BCL11B[42] as well as E-cadherin expression.[43][44]

MTA1 is a dual coregulatory as it stimulates the transcription of Stat3,[45] breast cancer-amplified sequence 3,[46] FosB,[25] paired box gene 5,[47] transglutaminase 2,[48]myeloid differentiation primary response 88,[49] tumor suppressorp14/p19ARF,[24][50]tyrosine hydroxylase,[51] clock gene CRY1,[29] SUMO2,[20] and Wnt1 and rhodopsin due to release of their transcriptional inhibition by homeodomain protein Six3,[41][52]

MTA1 interacts with ERα and coregulatory factors such as MAT1,[53] MICoA,[54]NRIF3 [55][55] and LMO4, [56],[56] which inhibits ER transactivation activity.[11] MTA1 also deacetylate its target proteins such as p53 and HIF and modulates their transactivation functions.[57][58] Furthermore, MTA1 could potentially modulate the expression of target genes through the microRNA network as MTA1 knockdown results modulation of miR-210, miR-125b, miR-194, miR-103, and miR-500.[59][60]

Cellular functions[edit]

MTA1 modulates the expression of target genes due to its ability to act as a corepressor or coactivator. MTA1 targets and/or effector pathways regulate pathways with cellular functions in both normal and cancer cells.[8][9] Physiological functions of MTA1 include: its role in the brain due to MTA1 interactions with DJ1[50] and endophilin-3;[61] regulation of Rhodopsin expression in the murine eye; modifier of circadian rhythm due to MTA1 interactions with the CLOCK-BMAL1 complex and stimulation of Cry-transcription; in heart development due to MTA1-FOG2 interaction; in mammary gland development as MTA1 depletion leads to ductal hypobranching, in spermatogenesis; in immunomodulation due to differential effects on the expression of cytokines in the resting and activated macrophage; in liver regeneration following hepatic injury; differentiation of mesenchymal stem cells into osteogenic axis; and a component of DNA-damage response.[8] In cancer cells, MTA1 and its downstream effectors regulate genes and/or pathways with roles in transformation, invasion, survival, angiogenesis, epithelial-to-mesenchymal transition, metastasis, DNA damage response, and hormone-independence of breast cancer.[6][9]

References[edit]

  1. ^ a b Toh Y, Pencil SD, Nicolson GL (Sep 1994). "A novel candidate metastasis-associated gene, mta1, differentially expressed in highly metastatic mammary adenocarcinoma cell lines. cDNA cloning, expression, and protein analyses". The Journal of Biological Chemistry 269 (37): 22958–63. PMID 8083195. 
  2. ^ a b Toh Y, Nicolson GL (Dec 2014). "Properties and clinical relevance of MTA1 protein in human cancer". Cancer Metastasis Reviews 33 (4): 891–900. doi:10.1007/s10555-014-9516-2. PMID 25359582. 
  3. ^ Liu J, Xu D, Wang H, Zhang Y, Chang Y, Zhang J, Wang J, Li C, Liu H, Zhao M, Lin C, Zhan Q, Huang C, Qian H (Jul 2014). "The subcellular distribution and function of MTA1 in cancer differentiation". Oncotarget 5 (13): 5153–64. doi:10.18632/oncotarget.2095. PMID 24970816. 
  4. ^ Liu J, Wang H, Huang C, Qian H (Dec 2014). "Subcellular localization of MTA proteins in normal and cancer cells". Cancer Metastasis Reviews 33 (4): 843–56. doi:10.1007/s10555-014-9511-7. PMID 25398252. 
  5. ^ a b Xue Y, Wong J, Moreno GT, Young MK, Côté J, Wang W (Dec 1998). "NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities". Molecular Cell 2 (6): 851–61. PMID 9885572. 
  6. ^ a b c d e f Li DQ, Kumar R (2015). "Unravelling the Complexity and Functions of MTA Coregulators in Human Cancer". Advances in Cancer Research 127: 1–47. doi:10.1016/bs.acr.2015.04.005. PMID 26093897. 
  7. ^ Kumar R, Gururaj AE (2008). "Coregulators as Oncogenes and Tumor Suppressors". In O'Malley BW, Kumar R. Nuclear Receptor Coregulators and Human Diseases. Hackensack, N.J.: World Scientific. pp. 195–218. doi:10.1142/9789812819178_0004. ISBN 978-981-281-917-8. 
  8. ^ a b c Sen N, Gui B, Kumar R (Dec 2014). "Physiological functions of MTA family of proteins". Cancer Metastasis Reviews 33 (4): 869–77. doi:10.1007/s10555-014-9514-4. PMID 25344801. 
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  10. ^ Kumar R (Dec 2014). "Functions and clinical relevance of MTA proteins in human cancer. Preface". Cancer Metastasis Reviews 33 (4): 835. doi:10.1007/s10555-014-9509-1. PMID 25348751. 
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  12. ^ a b Kumar R, Wang RA (May 2016). "Structure, expression and functions of MTA genes". Gene 582 (2): 112–21. doi:10.1016/j.gene.2016.02.012. PMID 26869315. 
  13. ^ a b Kleene R, Zdzieblo J, Wege K, Kern HF (Aug 1999). "A novel zymogen granule protein (ZG29p) and the nuclear protein MTA1p are differentially expressed by alternative transcription initiation in pancreatic acinar cells of the rat". Journal of Cell Science. 112 ( Pt 15): 2539–48. PMID 10393810. 
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  15. ^ a b c Millard CJ, Watson PJ, Celardo I, Gordiyenko Y, Cowley SM, Robinson CV, Fairall L, Schwabe JW (Jul 2013). "Class I HDACs share a common mechanism of regulation by inositol phosphates". Molecular Cell 51 (1): 57–67. doi:10.1016/j.molcel.2013.05.020. PMID 23791785. 
  16. ^ a b c Alqarni SS, Murthy A, Zhang W, Przewloka MR, Silva AP, Watson AA, Lejon S, Pei XY, Smits AH, Kloet SL, Wang H, Shepherd NE, Stokes PH, Blobel GA, Vermeulen M, Glover DM, Mackay JP, Laue ED (Aug 2014). "Insight into the architecture of the NuRD complex: structure of the RbAp48-MTA1 subcomplex". The Journal of Biological Chemistry 289 (32): 21844–55. doi:10.1074/jbc.M114.558940. PMID 24920672. 
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  52. ^ Manavathi B, Peng S, Rayala SK, Talukder AH, Wang MH, Wang RA, Balasenthil S, Agarwal N, Frishman LJ, Kumar R (Aug 2007). "Repression of Six3 by a corepressor regulates rhodopsin expression". Proceedings of the National Academy of Sciences of the United States of America 104 (32): 13128–33. doi:10.1073/pnas.0705878104. PMID 17666527. 
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  54. ^ Mishra SK, Mazumdar A, Vadlamudi RK, Li F, Wang RA, Yu W, Jordan VC, Santen RJ, Kumar R (May 2003). "MICoA, a novel metastasis-associated protein 1 (MTA1) interacting protein coactivator, regulates estrogen receptor-alpha transactivation functions". The Journal of Biological Chemistry 278 (21): 19209–19. doi:10.1074/jbc.M301968200. PMID 12639951. 
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  56. ^ Singh RR, Barnes CJ, Talukder AH, Fuqua SA, Kumar R (Nov 2005). "Negative regulation of estrogen receptor alpha transactivation functions by LIM domain only 4 protein". Cancer Research 65 (22): 10594–601. doi:10.1158/0008-5472.CAN-05-2268. PMID 16288053. 
  57. ^ Moon HE, Cheon H, Lee MS (Nov 2007). "Metastasis-associated protein 1 inhibits p53-induced apoptosis". Oncology Reports 18 (5): 1311–4. PMID 17914590. 
  58. ^ Moon HE, Cheon H, Chun KH, Lee SK, Kim YS, Jung BK, Park JA, Kim SH, Jeong JW, Lee MS (Oct 2006). "Metastasis-associated protein 1 enhances angiogenesis by stabilization of HIF-1alpha". Oncology Reports 16 (4): 929–35. PMID 16969516. 
  59. ^ Zhu X, Zhang X, Wang H, Song Q, Zhang G, Yang L, Geng J, Li X, Yuan Y, Chen L (Jul 2012). "MTA1 gene silencing inhibits invasion and alters the microRNA expression profile of human lung cancer cells". Oncology Reports 28 (1): 218–24. doi:10.3892/or.2012.1770. PMID 22576802. 
  60. ^ Li Y, Chao Y, Fang Y, Wang J, Wang M, Zhang H, Ying M, Zhu X, Wang H (29 May 2013). "MTA1 promotes the invasion and migration of non-small cell lung cancer cells by downregulating miR-125b". Journal of Experimental & Clinical Cancer Research 32: 33. doi:10.1186/1756-9966-32-33. PMID 23718732. 
  61. ^ Aramaki Y, Ogawa K, Toh Y, Ito T, Akimitsu N, Hamamoto H, Sekimizu K, Matsusue K, Kono A, Iguchi H, Takiguchi S (Jul 2005). "Direct interaction between metastasis-associated protein 1 and endophilin 3". FEBS Letters 579 (17): 3731–6. doi:10.1016/j.febslet.2005.05.069. PMID 15978591. 

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.