Submit
Search
Submit
Menu

  • Information

  • References

  • Contents

  • [1]N. A. Quaderi, S. Schweiger, K. Gaudenz, B. Franco, E. I. Rugarli, W. Berger, G. J. Feldman, M. Volta, G. Andolfi, S. Gilgenkrantz, R. W. Marion, R. C. Hennekam, J. M. Opitz, M. Muenke, H. H. Ropers and A. Ballabio: Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22. Nat Genet, 17(3), 285-91 (1997)

  • [2]A. Trockenbacher, V. Suckow, J. Foerster, J. Winter, S. Krauss, H. H. Ropers, R. Schneider and S. Schweiger: MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation. Nat Genet, 29(3), 287-94 (2001)

  • [3]E. Liu, C. A. Knutzen, S. Krauss, S. Schweiger and G. G. Chiang: Control of mTORC1 signaling by the Opitz syndrome protein MID1. Proc Natl Acad Sci U S A, 108(21), 8680-5 (2011)

  • [4]S. Krauss, J. Foerster, R. Schneider and S. Schweiger: Protein phosphatase 2A and rapamycin regulate the nuclear localization and activity of the transcription factor GLI3. Cancer Res, 68(12), 4658-65 (2008)

  • [5]B. Aranda-Orgilles, D. Rutschow, R. Zeller, A. I. Karagiannidis, A. Kohler, C. Chen, T. Wilson, S. Krause, S. Roepcke, D. Lilley, R. Schneider and S. Schweiger: Protein phosphatase 2A (PP2A)-specific ubiquitin ligase MID1 is a sequence-dependent regulator of translation efficiency controlling 3-phosphoinositide-dependent protein kinase-1 (PDPK-1). J Biol Chem, 286(46), 39945-57 (2011)

  • [6]Q. Zhang, S. M. Thomas, V. W. Lui, S. Xi, J. M. Siegfried, H. Fan, T. E. Smithgall, G. B. Mills and J. R. Grandis: Phosphorylation of TNF-alpha converting enzyme by gastrin-releasing peptide induces amphiregulin release and EGF receptor activation. Proc Natl Acad Sci U S A, 103(18), 6901-6 (2006)

  • [7]N. E. Bhola, M. L. Freilino, S. C. Joyce, M. Sen, S. M. Thomas, A. Sahu, A. Cassell, C. S. Chen and J. R. Grandis: Antitumor mechanisms of targeting the PDK1 pathway in head and neck cancer. Mol Cancer Ther, 11(6), 1236-46 (2012)

  • [8]A. Kohler, U. Demir, E. Kickstein, S. Krauss, J. Aigner, B. Aranda-Orgilles, A. I. Karagiannidis, C. Achmuller, H. Bu, A. Wunderlich, M. R. Schweiger, G. Schaefer, S. Schweiger, H. Klocker and R. Schneider: A hormone-dependent feedback-loop controls androgen receptor levels by limiting MID1, a novel translation enhancer and promoter of oncogenic signaling. Mol Cancer, 13, 146 (2014)

  • [9]M. M. Hettich, F. Matthes, D. P. Ryan, N. Griesche, S. Schroder, S. Dorn, S. Kraubeta and D. Ehninger: The anti-diabetic drug metformin reduces BACE1 protein level by interfering with the MID1 complex. PLoS One, 9(7), e102420 (2014)

  • [10]E. Kickstein, S. Krauss, P. Thornhill, D. Rutschow, R. Zeller, J. Sharkey, R. Williamson, M. Fuchs, A. Kohler, H. Glossmann, R. Schneider, C. Sutherland and S. Schweiger: Biguanide metformin acts on tau phosphorylation via mTOR/protein phosphatase 2A (PP2A) signaling. Proc Natl Acad Sci U S A, 107(50), 21830-5 (2010)

  • [11]S. Krauss, N. Griesche, E. Jastrzebska, C. Chen, D. Rutschow, C. Achmuller, S. Dorn, S. M. Boesch, M. Lalowski, E. Wanker, R. Schneider and S. Schweiger: Translation of HTT mRNA with expanded CAG repeats is regulated by the MID1-PP2A protein complex. Nat Commun, 4, 1511 (2013)

  • [12]U. Demir, A. Koehler, R. Schneider, S. Schweiger and H. Klocker: Metformin anti-tumor effect via disruption of the MID1 translational regulator complex and AR downregulation in prostate cancer cells. BMC Cancer, 14, 52 (2014)

  • [13]J. Winter, T. Lehmann, S. Krauss, A. Trockenbacher, Z. Kijas, J. Foerster, V. Suckow, M. L. Yaspo, A. Kulozik, V. Kalscheuer, R. Schneider and S. Schweiger: Regulation of the MID1 protein function is fine-tuned by a complex pattern of alternative splicing. Hum Genet, 114(6), 541-52 (2004)

  • [14]J. Winter, M. Kunath, S. Roepcke, S. Krause, R. Schneider and S. Schweiger: Alternative polyadenylation signals and promoters act in concert to control tissue-specific expression of the Opitz Syndrome gene MID1. BMC Mol Biol, 8, 105 (2007)

  • [15]K. M. Short, B. Hopwood, Z. Yi and T. C. Cox: MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders. BMC Cell Biol, 3, 1 (2002)

  • [16]S. Schweiger, J. Foerster, T. Lehmann, V. Suckow, Y. A. Muller, G. Walter, T. Davies, H. Porter, H. van Bokhoven, P. W. Lunt, P. Traub and H. H. Ropers: The Opitz syndrome gene product, MID1, associates with microtubules. Proc Natl Acad Sci U S A, 96(6), 2794-9 (1999)

  • [17]B. Aranda-Orgilles, J. Aigner, M. Kunath, R. Lurz, R. Schneider and S. Schweiger: Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A. PLoS One, 3(10), e3507 (2008)

  • [18]C. A. Joazeiro and A. M. Weissman: RING finger proteins: mediators of ubiquitin ligase activity. Cell, 102(5), 549-52 (2000)

  • [19]J. Liu, T. D. Prickett, E. Elliott, G. Meroni and D. L. Brautigan: Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4. Proc Natl Acad Sci U S A, 98(12), 6650-5 (2001)

  • [20]H. Du, Y. Huang, M. Zaghlula, E. Walters, T. C. Cox and M. A. Massiah: The MID1 E3 ligase catalyzes the polyubiquitination of Alpha4 (alpha4), a regulatory subunit of protein phosphatase 2A (PP2A): novel insights into MID1-mediated regulation of PP2A. J Biol Chem, 288(29), 21341-50 (2013)

  • [21]G. R. Watkins, N. Wang, M. D. Mazalouskas, R. J. Gomez, C. R. Guthrie, B. C. Kraemer, S. Schweiger, B. W. Spiller and B. E. Wadzinski: Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phosphorylation. J Biol Chem, 287(29), 24207-15 (2012)

  • [22]S. Schweiger, S. Dorn, M. Fuchs, A. Kohler, F. Matthes, E. C. Muller, E. Wanker, R. Schneider and S. Krauss: The E3 Ubiquitin Ligase MID1 Catalyzes Ubiquitination and Cleavage of Fu. J Biol Chem, 289(46), 31805-17 (2014)

  • [23]S. Sengupta, T. R. Peterson and D. M. Sabatini: Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress. Mol Cell, 40(2), 310-22 (2010)

  • [24]B. Aranda-Orgilles, A. Trockenbacher, J. Winter, J. Aigner, A. Kohler, E. Jastrzebska, J. Stahl, E. C. Muller, A. Otto, E. E. Wanker, R. Schneider and S. Schweiger: The Opitz syndrome gene product MID1 assembles a microtubule-associated ribonucleoprotein complex. Hum Genet, 123(2), 163-76 (2008)

  • [25]J. Opitz, R. Summit and D. Smith: The BBB syndrome: Familial telecanthus with associated congenital anomalies. Birth Defects: Original Article Series, 2, 86-94 (1969)

  • [26]J. Opitz, J. Frias, J. Gutenberger and J. Pellet: The G-syndrome of multiple congenital anomalies. Birth Defects: Original Article Series, 2, 95-101 (1969)

  • [27]V. McKusick, C. Francomano and S. E. Antonarakis: Mendelian Inheritance in Man. Baltimore: John Hopkins University Press., 11th ed. (1995)

  • [28]J. F. Cordero and L. B. Holmes: Phenotypic overlap of the BBB and G syndromes. Am J Med Genet, 2(2), 145-52 (1978)

  • [29]N. H. Robin, G. J. Feldman, A. L. Aronson, H. F. Mitchell, R. Weksberg, C. O. Leonard, B. K. Burton, K. D. Josephson, R. Laxova, K. A. Aleck, J. E. Allanson, M. L. Guion-Almeida, R. A. Martin, L. G. Leichtman, R. A. Price, J. M. Opitz and M. Muenke: Opitz syndrome is genetically heterogeneous, with one locus on Xp22, and a second locus on 22q11.2. Nat Genet, 11(4), 459-61 (1995)

  • [30]P. Kruszka, D. Li, M. H. Harr, N. R. Wilson, D. Swarr, E. M. McCormick, R. M. Chiavacci, M. Li, A. F. Martinez, R. A. Hart, D. M. McDonald-McGinn, M. A. Deardorff, M. J. Falk, J. E. Allanson, C. Hudson, J. P. Johnson, I. Saadi, H. Hakonarson, M. Muenke and E. H. Zackai: Mutations in SPECC1L, encoding sperm antigen with calponin homology and coiled-coil domains 1-like, are found in some cases of autosomal dominant Opitz G/BBB syndrome. J Med Genet (2014)

  • [31]I. Saadi, F. S. Alkuraya, S. S. Gisselbrecht, W. Goessling, R. Cavallesco, A. Turbe-Doan, A. L. Petrin, J. Harris, U. Siddiqui, A. W. Grix, Jr., H. D. Hove, P. Leboulch, T. W. Glover, C. C. Morton, A. Richieri-Costa, J. C. Murray, R. P. Erickson and R. L. Maas: Deficiency of the cytoskeletal protein SPECC1L leads to oblique facial clefting. Am J Hum Genet, 89(1), 44-55 (2011)

  • [32]J. S. Fryburg, K. Y. Lin and W. L. Golden: Chromosome 22q11.2. deletion in a boy with Opitz (G/BBB) syndrome. Am J Med Genet, 62(3), 274-5 (1996)

  • [33]Y. Lacassie and M. I. Arriaza: Opitz GBBB syndrome and the 22q11.2. deletion. Am J Med Genet, 62(3), 318 (1996)

  • [34]D. M. McDonald-McGinn, D. A. Driscoll, L. Bason, K. Christensen, D. Lynch, K. Sullivan, D. Canning, W. Zavod, N. Quinn and J. Rome: Autosomal dominant “Opitz” GBBB syndrome due to a 22q11.2. deletion. Am J Med Genet, 59(1), 103-13 (1995)

  • [35]I. B. Van den Veyver, T. A. Cormier, V. Jurecic, A. Baldini and H. Y. Zoghbi: Characterization and physical mapping in human and mouse of a novel RING finger gene in Xp22. Genomics, 51(2), 251-61 (1998)

  • [36]A. N. Sferruzzi-Perri, A. M. Macpherson, C. T. Roberts and S. A. Robertson: Csf2 null mutation alters placental gene expression and trophoblast glycogen cell and giant cell abundance in mice. Biol Reprod, 81(1), 207-21 (2009)

  • [37]S. Palmer, J. Perry, D. Kipling and A. Ashworth: A gene spans the pseudoautosomal boundary in mice. Proc Natl Acad Sci U S A, 94(22), 12030-5 (1997)

  • [38]S. Yokoyama, Y. Ito, H. Ueno-Kudoh, H. Shimizu, K. Uchibe, S. Albini, K. Mitsuoka, S. Miyaki, M. Kiso, A. Nagai, T. Hikata, T. Osada, N. Fukuda, S. Yamashita, D. Harada, V. Mezzano, M. Kasai, P. L. Puri, Y. Hayashizaki, H. Okado, M. Hashimoto and H. Asahara: A systems approach reveals that the myogenesis genome network is regulated by the transcriptional repressor RP58. Dev Cell, 17(6), 836-48 (2009)

  • [39]P. A. Gray, H. Fu, P. Luo, Q. Zhao, J. Yu, A. Ferrari, T. Tenzen, D. I. Yuk, E. F. Tsung, Z. Cai, J. A. Alberta, L. P. Cheng, Y. Liu, J. M. Stenman, M. T. Valerius, N. Billings, H. A. Kim, M. E. Greenberg, A. P. McMahon, D. H. Rowitch, C. D. Stiles and Q. Ma: Mouse brain organization revealed through direct genome-scale TF expression analysis. Science, 306(5705), 2255-7 (2004)

  • [40]G. Diez-Roux, S. Banfi, M. Sultan, L. Geffers, S. Anand, D. Rozado, A. Magen, E. Canidio, M. Pagani, I. Peluso, N. Lin-Marq, M. Koch, M. Bilio, I. Cantiello, R. Verde, C. De Masi, S. A. Bianchi, J. Cicchini, E. Perroud, S. Mehmeti, E. Dagand, S. Schrinner, A. Nurnberger, K. Schmidt, K. Metz, C. Zwingmann, N. Brieske, C. Springer, A. M. Hernandez, S. Herzog, F. Grabbe, C. Sieverding, B. Fischer, K. Schrader, M. Brockmeyer, S. Dettmer, C. Helbig, V. Alunni, M. A. Battaini, C. Mura, C. N. Henrichsen, R. Garcia-Lopez, D. Echevarria, E. Puelles, E. Garcia-Calero, S. Kruse, M. Uhr, C. Kauck, G. Feng, N. Milyaev, C. K. Ong, L. Kumar, M. Lam, C. A. Semple, A. Gyenesei, S. Mundlos, U. Radelof, H. Lehrach, P. Sarmientos, A. Reymond, D. R. Davidson, P. Dolle, S. E. Antonarakis, M. L. Yaspo, S. Martinez, R. A. Baldock, G. Eichele and A. Ballabio: A high-resolution anatomical atlas of the transcriptome in the mouse embryo. PLoS Biol, 9(1), e1000582 (2011)

  • [41]G. Consortium: GUDMAP: the GenitoUrinary Development Molecular Anatomy Project. http://www.gudmap.org (2004)

  • [42]B. Fontanella, G. Russolillo and G. Meroni: MID1 mutations in patients with X-linked Opitz G/BBB syndrome. Hum Mutat, 29(5), 584-94 (2008)

  • [43]T. Lu, R. Chen, T. C. Cox, R. X. Moldrich, N. Kurniawan, G. Tan, J. K. Perry, A. Ashworth, P. F. Bartlett, L. Xu, J. Zhang, B. Lu, M. Wu, Q. Shen, Y. Liu, L. J. Richards and Z. Xiong: X-linked microtubule-associated protein, Mid1, regulates axon development. Proc Natl Acad Sci U S A, 110(47), 19131-6 (2013)

  • [44]A. Lancioni, M. Pizzo, B. Fontanella, R. Ferrentino, L. M. Napolitano, E. De Leonibus and G. Meroni: Lack of Mid1, the mouse ortholog of the Opitz syndrome gene, causes abnormal development of the anterior cerebellar vermis. J Neurosci, 30(8), 2880-7 (2010)

  • [45]P. A. Trainor: Neural Crest Cells: Evolution, Development and Disease. In: Academic Press Elsevier, (2014)

  • [46]L. Pinson, J. Auge, S. Audollent, G. Mattei, H. Etchevers, N. Gigarel, F. Razavi, D. Lacombe, S. Odent, M. Le Merrer, J. Amiel, A. Munnich, G. Meroni, S. Lyonnet, M. Vekemans and T. Attie-Bitach: Embryonic expression of the human MID1 gene and its mutations in Opitz syndrome. J Med Genet, 41(5), 381-6 (2004)

  • [47]J. M. Richman, K. K. Fu, L. L. Cox, J. P. Sibbons and T. C. Cox: Isolation and characterisation of the chick orthologue of the Opitz syndrome gene, Mid1, supports a conserved role in vertebrate development. Int J Dev Biol, 46(4), 441-8 (2002)

  • [48]E. J. Latta and J. P. Golding: Regulation of PP2A activity by Mid1 controls cranial neural crest speed and gangliogenesis. Mech Dev, 128(11-12), 560-76 (2012)

  • [49]A. Granata and N. A. Quaderi: The Opitz syndrome gene MID1 is essential for establishing asymmetric gene expression in Hensen’s node. Dev Biol, 258(2), 397-405 (2003)

  • [50]S. R. Twigg, R. Kan, C. Babbs, E. G. Bochukova, S. P. Robertson, S. A. Wall, G. M. Morriss-Kay and A. O. Wilkie: Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome. Proc Natl Acad Sci U S A, 101(23), 8652-7 (2004)

  • [51]I. Wieland, S. Jakubiczka, P. Muschke, M. Cohen, H. Thiele, K. L. Gerlach, R. H. Adams and P. Wieacker: Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome. Am J Hum Genet, 74(6), 1209-15 (2004)

  • [52]A. Davy, J. Aubin and P. Soriano: Ephrin-B1 forward and reverse signaling are required during mouse development. Genes Dev, 18(5), 572-83 (2004)

  • [53]A. Davy, J. O. Bush and P. Soriano: Inhibition of gap junction communication at ectopic Eph/ephrin boundaries underlies craniofrontonasal syndrome. PLoS Biol, 4(10), e315 (2006)

  • [54]J. O. Bush and P. Soriano: Ephrin-B1 forward signaling regulates craniofacial morphogenesis by controlling cell proliferation across Eph-ephrin boundaries. Genes Dev, 24(18), 2068-80 (2010)

  • [55]B. Aranda-Orgilles: Characterisation of the MID1/α4 multiprotein complex. PhD Thesis, Freie Universität, Berlin (2006)

  • [56]M. Murone, A. Rosenthal and F. J. de Sauvage: Hedgehog signal transduction: from flies to vertebrates. Exp Cell Res, 253(1), 25-33 (1999)

  • [57]S. A. Brugmann, N. C. Allen, A. W. James, Z. Mekonnen, E. Madan and J. A. Helms: A primary cilia-dependent etiology for midline facial disorders. Hum Mol Genet, 19(8), 1577-92 (2010)

  • [58]A. Vortkamp, M. Gessler and K. H. Grzeschik: GLI3 zinc-finger gene interrupted by translocations in Greig syndrome families. Nature, 352(6335), 539-40 (1991)

  • [59]A. Wild, M. Kalff-Suske, A. Vortkamp, D. Bornholdt, R. Konig and K. H. Grzeschik: Point mutations in human GLI3 cause Greig syndrome. Hum Mol Genet, 6(11), 1979-84 (1997)

  • [60]S. Krauss, J. So, M. Hambrock, A. Kohler, M. Kunath, C. Scharff, M. Wessling, K. H. Grzeschik, R. Schneider and S. Schweiger: Point mutations in GLI3 lead to misregulation of its subcellular localization. PLoS One, 4(10), e7471 (2009)

  • [61]S. Martinez, A. Andreu, N. Mecklenburg and D. Echevarria: Cellular and molecular basis of cerebellar development. Front Neuroanat, 7, 18 (2013)

  • [62]J. Xu, Z. Liu and D. M. Ornitz: Temporal and spatial gradients of Fgf8 and Fgf17 regulate proliferation and differentiation of midline cerebellar structures. Development, 127(9), 1833-43 (2000)

  • [63]S. Blaess, D. Stephen and A. L. Joyner: Gli3 coordinates three-dimensional patterning and growth of the tectum and cerebellum by integrating Shh and Fgf8 signaling. Development, 135(12), 2093-103 (2008)

  • [64]S. Blaess, J. D. Corrales and A. L. Joyner: Sonic hedgehog regulates Gli activator and repressor functions with spatial and temporal precision in the mid/hindbrain region. Development, 133(9), 1799-809 (2006)

  • [65]S. Sundaram, A. H. Huq, T. Hsia and H. Chugani: Exome sequencing and diffusion tensor imaging in developmental disabilities. Pediatr Res, 75(3), 443-7 (2014)

  • [66]L. J. Paulozzi, J. D. Erickson and R. J. Jackson: Hypospadias trends in two US surveillance systems. Pediatrics, 100(5), 831-4 (1997)

  • [67]S. L. Carmichael, G. M. Shaw and E. J. Lammer: Environmental and genetic contributors to hypospadias: a review of the epidemiologic evidence. Birth Defects Res A Clin Mol Teratol, 94(7), 499-510 (2012)

  • [68]B. Gottlieb, L. K. Beitel, A. Nadarajah, M. Paliouras and M. Trifiro: The androgen receptor gene mutations database: 2012 update. Hum Mutat, 33(5), 887-94 (2012)

  • [69]S. Miyagawa, Y. Satoh, R. Haraguchi, K. Suzuki, T. Iguchi, M. M. Taketo, N. Nakagata, T. Matsumoto, K. Takeyama, S. Kato and G. Yamada: Genetic interactions of the androgen and Wnt/beta-catenin pathways for the masculinization of external genitalia. Mol Endocrinol, 23(6), 871-80 (2009)

  • [70]R. Haraguchi, R. Mo, C. Hui, J. Motoyama, S. Makino, T. Shiroishi, W. Gaffield and G. Yamada: Unique functions of Sonic hedgehog signaling during external genitalia development. Development, 128(21), 4241-50 (2001)

  • [71]C. Wetmore: Sonic hedgehog in normal and neoplastic proliferation: insight gained from human tumors and animal models. Curr Opin Genet Dev, 13(1), 34-42 (2003)

  • [72]D. M. Berman, S. S. Karhadkar, A. Maitra, R. Montes De Oca, M. R. Gerstenblith, K. Briggs, A. R. Parker, Y. Shimada, J. R. Eshleman, D. N. Watkins and P. A. Beachy: Widespread requirement for Hedgehog ligand stimulation in growth of digestive tract tumours. Nature, 425(6960), 846-51 (2003)

  • [73]D. N. Watkins, D. M. Berman, S. G. Burkholder, B. Wang, P. A. Beachy and S. B. Baylin: Hedgehog signalling within airway epithelial progenitors and in small-cell lung cancer. Nature, 422(6929), 313-7 (2003)

  • [74]S. P. Thayer, M. P. di Magliano, P. W. Heiser, C. M. Nielsen, D. J. Roberts, G. Y. Lauwers, Y. P. Qi, S. Gysin, C. Fernandez-del Castillo, V. Yajnik, B. Antoniu, M. McMahon, A. L. Warshaw and M. Hebrok: Hedgehog is an early and late mediator of pancreatic cancer tumorigenesis. Nature, 425(6960), 851-6 (2003)

  • [75]P. Sanchez, A. M. Hernandez, B. Stecca, A. J. Kahler, A. M. DeGueme, A. Barrett, M. Beyna, M. W. Datta, S. Datta and A. Ruiz i Altaba: Inhibition of prostate cancer proliferation by interference with SONIC HEDGEHOG-GLI1 signaling. Proc Natl Acad Sci U S A, 101(34), 12561-6 (2004)

  • [76]D. A. Bastos, C. Dzik, D. Rathkopf and H. I. Scher: Expanding androgen- and androgen receptor signaling-directed therapies for castration-resistant prostate cancer. Oncology (Williston Park), 28(8), 693-9 (2014)

  • [77]A. Mora, D. Komander, D. M. van Aalten and D. R. Alessi: PDK1, the master regulator of AGC kinase signal transduction. Semin Cell Dev Biol, 15(2), 161-70 (2004)

  • [78]R. J. Dowling, I. Topisirovic, T. Alain, M. Bidinosti, B. D. Fonseca, E. Petroulakis, X. Wang, O. Larsson, A. Selvaraj, Y. Liu, S. C. Kozma, G. Thomas and N. Sonenberg: mTORC1-mediated cell proliferation, but not cell growth, controlled by the 4E-BPs. Science, 328(5982), 1172-6 (2010)

  • [79]C. Sanchez Canedo, B. Demeulder, A. Ginion, J. R. Bayascas, J. L. Balligand, D. R. Alessi, J. L. Vanoverschelde, C. Beauloye, L. Hue and L. Bertrand: Activation of the cardiac mTOR/p70(S6K) pathway by leucine requires PDK1 and correlates with PRAS40 phosphorylation. Am J Physiol Endocrinol Metab, 298(4), E761-9 (2010)

  • [80]M. Arigoni, G. Barutello, F. Riccardo, E. Ercole, D. Cantarella, F. Orso, L. Conti, S. Lanzardo, D. Taverna, I. Merighi, R. A. Calogero, F. Cavallo and E. Quaglino: miR-135b coordinates progression of ErbB2-driven mammary carcinomas through suppression of MID1 and MTCH2. Am J Pathol, 182(6), 2058-70 (2013)

  • [81]C. P. Ferri, M. Prince, C. Brayne, H. Brodaty, L. Fratiglioni, M. Ganguli, K. Hall, K. Hasegawa, H. Hendrie, Y. Huang, A. Jorm, C. Mathers, P. R. Menezes, E. Rimmer, M. Scazufca and I. Alzheimer’s Disease: Global prevalence of dementia: a Delphi consensus study. Lancet, 366(9503), 2112-7 (2005)

  • [82]A. Alzheimer, R. A. Stelzmann, H. N. Schnitzlein and F. R. Murtagh: An English translation of Alzheimer’s 1907 paper, “Uber eine eigenartige Erkankung der Hirnrinde”. Clin Anat, 8(6), 429-31 (1995)

  • [83]Y. W. Zhang, R. Thompson, H. Zhang and H. Xu: APP processing in Alzheimer’s disease. Mol Brain, 4, 3 (2011)

  • [84]G. M. Shankar and D. M. Walsh: Alzheimer’s disease: synaptic dysfunction and Abeta. Mol Neurodegener, 4, 48 (2009)

  • [85]A. D. Alonso, I. Grundke-Iqbal, H. S. Barra and K. Iqbal: Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau. Proc Natl Acad Sci U S A, 94(1), 298-303 (1997)

  • [86]C. X. Gong, F. Liu, I. Grundke-Iqbal and K. Iqbal: Post-translational modifications of tau protein in Alzheimer’s disease. J Neural Transm, 112(6), 813-38 (2005)

  • [87]Q. Tian and J. Wang: Role of serine/threonine protein phosphatase in Alzheimer’s disease. Neurosignals, 11(5), 262-9 (2002)

  • [88]C. X. Gong, T. J. Singh, I. Grundke-Iqbal and K. Iqbal: Phosphoprotein phosphatase activities in Alzheimer disease brain. J Neurochem, 61(3), 921-7 (1993)

  • [89]C. X. Gong, S. Shaikh, J. Z. Wang, T. Zaidi, I. Grundke-Iqbal and K. Iqbal: Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain. J Neurochem, 65(2), 732-8 (1995)

  • [90]V. Vogelsberg-Ragaglia, T. Schuck, J. Q. Trojanowski and V. M. Lee: PP2A mRNA expression is quantitatively decreased in Alzheimer’s disease hippocampus. Exp Neurol, 168(2), 402-12 (2001)

  • [91]J. F. Loring, X. Wen, J. M. Lee, J. Seilhamer and R. Somogyi: A gene expression profile of Alzheimer’s disease. DNA Cell Biol, 20(11), 683-95 (2001)

  • [92]E. Sontag, A. Luangpirom, C. Hladik, I. Mudrak, E. Ogris, S. Speciale and C. L. White, 3rd: Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer disease pathology. J Neuropathol Exp Neurol, 63(4), 287-301 (2004)

  • [93]K. Iqbal, F. Liu, C. X. Gong, C. Alonso Adel and I. Grundke-Iqbal: Mechanisms of tau-induced neurodegeneration. Acta Neuropathol, 118(1), 53-69 (2009)

  • [94]J. Li, J. Deng, W. Sheng and Z. Zuo: Metformin attenuates Alzheimer’s disease-like neuropathology in obese, leptin-resistant mice. Pharmacol Biochem Behav, 101(4), 564-74 (2012)

  • [95]A. Gupta, B. Bisht and C. S. Dey: Peripheral insulin-sensitizer drug metformin ameliorates neuronal insulin resistance and Alzheimer’s-like changes. Neuropharmacology, 60(6), 910-20 (2011)

  • [96]Y. Chen, K. Zhou, R. Wang, Y. Liu, Y. D. Kwak, T. Ma, R. C. Thompson, Y. Zhao, L. Smith, L. Gasparini, Z. Luo, H. Xu and F. F. Liao: Antidiabetic drug metformin (GlucophageR) increases biogenesis of Alzheimer’s amyloid peptides via up-regulating BACE1 transcription. Proc Natl Acad Sci U S A, 106(10), 3907-12 (2009)

  • [97]P. Imfeld, M. Bodmer, S. S. Jick and C. R. Meier: Metformin, other antidiabetic drugs, and risk of Alzheimer’s disease: a population-based case-control study. J Am Geriatr Soc, 60(5), 916-21 (2012)

  • [98]J. M. Gil and A. C. Rego: Mechanisms of neurodegeneration in Huntington’s disease. Eur J Neurosci, 27(11), 2803-20 (2008)

  • [99]M. DiFiglia, E. Sapp, K. O. Chase, S. W. Davies, G. P. Bates, J. P. Vonsattel and N. Aronin: Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science, 277(5334), 1990-3 (1997)

  • [100]E. Scherzinger, R. Lurz, M. Turmaine, L. Mangiarini, B. Hollenbach, R. Hasenbank, G. P. Bates, S. W. Davies, H. Lehrach and E. E. Wanker: Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell, 90(3), 549-58 (1997)

  • [101]C. M. Everett and N. W. Wood: Trinucleotide repeats and neurodegenerative disease. Brain, 127(Pt 11), 2385-405 (2004)

  • [102]D. C. Rubinsztein: How does the Huntington’s disease mutation damage cells? Sci Aging Knowledge Environ, 2003(37), PE26 (2003)

  • [103]J. T. den Dunnen and S. E. Antonarakis: Mutation nomenclature extensions and suggestions to describe complex mutations: a discussion. Hum Mutat, 15(1), 7-12 (2000)

  • [104]C. Migliore, E. Athanasakis, S. Dahoun, A. Wonkam, M. Lees, O. Calabrese, F. Connell, S. A. Lynch, C. Izzi, E. Pompilii, S. Thakur, M. van Maarle, L. C. Wilson and G. Meroni: Complex rearrangement of the exon 6 genomic region among Opitz G/BBB Syndrome MID1 alterations. Eur J Med Genet, 56(8), 404-10 (2013)

  • [105]C. H. Hu, Y. F. Liu, J. S. Yu, Y. Y. Ng, S. J. Chen, P. H. Su and J. Y. Chen: A MID1 gene mutation in a patient with Opitz G/BBB syndrome that altered the 3D structure of SPRY domain. Am J Med Genet A, 158A(4), 726-31 (2012)

  • [106]R. Ferrentino, M. T. Bassi, D. Chitayat, E. Tabolacci and G. Meroni: MID1 mutation screening in a large cohort of Opitz G/BBB syndrome patients: twenty-nine novel mutations identified. Hum Mutat, 28(2), 206-7 (2007)

  • [107]E. W. Hsieh, K. Vargervik and A. M. Slavotinek: Clinical and molecular studies of patients with characteristics of Opitz G/BBB syndrome shows a novel MID1 mutation. Am J Med Genet A, 146A(18), 2337-45 (2008)

  • [108]I. Huning, K. Kutsche, S. Rajaei, A. Erlandsson, L. Lovmar, J. Rundberg and M. Stefanova: Exon 2 duplication of the MID1 gene in a patient with a mild phenotype of Opitz G/BBB syndrome. Eur J Med Genet, 56(4), 188-91 (2013)

  • [109]X. Ji, Y. Xing, Y. Xu, Y. Liu, Y. Chen, J. Tao and B. Xiao: A novel mutation in MID1 in a patient with X-linked Opitz G/BBB syndrome. Gene, 537(1), 140-2 (2014)

Article Metrics

  • Information

  • Download

  • Contents

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

1 Jan 2016Review
The MID1 protein is a central player during development and in disease
Jennifer Winter 1, M. Felicia Basilicata 2,3, Marc P. Stemmler 2,4, Sybille Krauss 5,*
Affiliations
Article Info

1 Institute of Human Genetics University Medical Centre of the Johannes Gutenberg University, Langenbeckstr. 1, 55131 Mainz, Germany

2 Department of Molecular Embryology, Max Planck Institute of Immunobiology and Epigenetics, Stuebeweg 51, 79108 Freiburg, Germany

3 Department of Chromatin Regulation, Max Planck Institute of Immunobiology and Epigenetics, 79108 Freiburg, Germany

4 Department of Experimental Medicine I, Nikolaus-Fiebiger Center for Molecular Medicine, Friedrich-Alexander University, 90154 Erlangen, Germany

5 German Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Str.25, 53127 Bonn, Germany

Abstract

Loss-of-function mutations in the MID1 gene cause a rare monogenic disorder, Opitz BBB/G syndrome (OS), which is characterized by malformations of the ventral midline. The MID1 gene encodes the MID1 protein, which assembles a large microtubule-associated protein complex. Intensive research over the past several years has shed light on the function of the MID1 protein as a ubiquitin ligase and regulator of mTOR signalling and translational activator. As a central player in the cell MID1 has been implicated in the pathogenesis of various other disorders in addition to OS including cancer and neurodegenerative diseases. Influencing the activity of the MID1 protein complex is a promising new strategy for the treatment of these diseases. In this review we will summarize the current knowledge about MID1, its involvement in the pathogenesis of OS and other diseases and possible strategies for therapy development.

Keywords

  • MID1
  • Opitz BBB/G Syndrome
  • mTOR
  • PP2A
  • SHH
  • Review

References