The neurobiology of the dystrophin-associated glycoprotein complex

References

• Davies KE, Nowak KJ. Molecular mechanisms of muscular dystrophies: old and new players. Nat Rev Mol Cell Biol 2006; 7: 762–73
   PubMed Web of Science ®Google Scholar
• Yoshida M, Suzuki A, Yamamoto H, Noguchi S, Mizuno Y, Ozawa E. Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside. Eur J Biochem 1994; 222: 1055–61
   PubMedGoogle Scholar
• Blake DJ, Weir A, Newey SE, Davies KE. Function and genetics of dystrophin and dystrophin-related proteins in muscle. Physiol Rev 2002; 82: 291–329
   PubMed Web of Science ®Google Scholar
• Hopf FW, Turner PR, Steinhardt RA. Calcium misregulation and the pathogenesis of muscular dystrophy. Subcell Biochem 2007; 45: 429–64
   PubMedGoogle Scholar
• Batchelor CL, Winder SJ. Sparks, signals and shock absorbers: how dystrophin loss causes muscular dystrophy. Trends Cell Biol 2006; 16: 198–205
   PubMedGoogle Scholar
• Ervasti JM. Dystrophin, its interactions with other proteins, and implications for muscular dystrophy. Biochim Biophys Acta 2007; 1772: 108–17
   PubMed Web of Science ®Google Scholar
• Nowak KJ, Davies KE. Duchenne muscular dystrophy and dystrophin: pathogenesis and opportunities for treatment. EMBO Rep 2004; 5: 872–6
   PubMed Web of Science ®Google Scholar
• Mehler MF. Brain dystrophin, neurogenetics and mental retardation. Brain Res Brain Res Rev 2000; 32: 277–307
   PubMedGoogle Scholar
• Cotton SM, Voudouris NJ, Greenwood KM. Association between intellectual functioning and age in children and young adults with Duchenne muscular dystrophy: further results from a meta-analysis. Dev Med Child Neurol 2005; 47: 257–65
   PubMed Web of Science ®Google Scholar
• Billard C, Gillet P, Barthez M, Hommet C, Bertrand P. Reading ability and processing in Duchenne muscular dystrophy and spinal muscular atrophy. Dev Med Child Neurol 1998; 40: 12–20
   PubMed Web of Science ®Google Scholar
• Moizard MP, Toutain A, Fournier D, Berret F, Raynaud M, Billard C, et al. Severe cognitive impairment in DMD: obvious clinical indication for Dp71 isoform point mutation screening. Eur J Hum Genet 2000; 8: 552–6
   Google Scholar
• Lenk U, Hanke R, Thiele H, Speer A. Point mutations at the carboxy terminus of the human dystrophin gene: implications for an association with mental retardation in DMD patients. Hum Mol Genet 1993; 2: 1877–81
   PubMed Web of Science ®Google Scholar
• Wibawa T, Takeshima Y, Mitsuyoshi I, Wada H, Surono A, Nakamura H, et al. Complete skipping of exon 66 due to novel mutations of the dystrophin gene was identified in two Japanese families of Duchenne muscular dystrophy with severe mental retardation. Brain Dev 2000; 22: 107–12
   Google Scholar
• Hendriksen JG, Vles JS. Neuropsychiatric disorders in males with duchenne muscular dystrophy: frequency rate of attention-deficit hyperactivity disorder (ADHD), autism spectrum disorder, and obsessive-compulsive disorder. J Child Neurol 2008; 23: 477–81
   PubMed Web of Science ®Google Scholar
• Hinton VJ, Nereo NE, Fee RJ, Cyrulnik SE. Social behavior problems in boys with Duchenne muscular dystrophy. J Dev Behav Pediatr 2006; 27: 470–6
   PubMed Web of Science ®Google Scholar
• Poysky J. Behavior patterns in Duchenne muscular dystrophy: report on the Parent Project Muscular Dystrophy behavior workshop 8–9 of December 2006, Philadelphia, USA. Neuromuscul Disord 2007; 17: 986–94
   PubMedGoogle Scholar
• Lee JS, Pfund Z, Juhasz C, Behen ME, Muzik O, Chugani DC, et al. Altered regional brain glucose metabolism in Duchenne muscular dystrophy: a pet study. Muscle Nerve 2002; 26: 506–12
   PubMed Web of Science ®Google Scholar
• Tracey I, Scott RB, Thompson CH, Dunn JF, Barnes PR, Styles P, et al. Brain abnormalities in Duchenne muscular dystrophy: phosphorus-31 magnetic resonance spectroscopy and neuropsychological study. Lancet 1995; 345: 1260–4
   PubMed Web of Science ®Google Scholar
• Blake DJ, Hawkes R, Benson MA, Beesley PW. Different dystrophin-like complexes are expressed in neurons and glia. J Cell Biol 1999; 147: 645–58
   PubMedGoogle Scholar
• Moukhles H, Carbonetto S. Dystroglycan contributes to the formation of multiple dystrophin-like complexes in brain. J Neurochem 2001; 78: 824–34
   Google Scholar
• Gorecki DC, Monaco AP, Derry JM, Walker AP, Barnard EA, Barnard PJ. Expression of four alternative dystrophin transcripts in brain regions regulated by different promoters. Hum Mol Genet 1992; 1: 505–10
   PubMed Web of Science ®Google Scholar
• Blake DJ, Love DR, Tinsley J, Morris GE, Turley H, Gatter K, et al. Characterization of a 4.8kb transcript from the Duchenne muscular dystrophy locus expressed in Schwannoma cells. Hum Mol Genet 1992; 1: 103–9
   PubMedGoogle Scholar
• Lederfein D, Yaffe D, Nudel U. A housekeeping type promoter, located in the 3' region of the Duchenne muscular dystrophy gene, controls the expression of Dp71, a major product of the gene. Hum Mol Genet 1993; 2: 1883–8
   Google Scholar
• Lidov HG, Selig S, Kunkel LM. Dp140: a novel 140 kDa CNS transcript from the dystrophin locus. Hum Mol Genet 1995; 4: 329–35
   PubMed Web of Science ®Google Scholar
• Lidov HG, Byers TJ, Watkins SC, Kunkel LM. Localization of dystrophin to postsynaptic regions of central nervous system cortical neurons. Nature 1990; 348: 725–8
   PubMed Web of Science ®Google Scholar
• Knuesel I, Mastrocola M, Zuellig RA, Bornhauser B, Schaub MC, Fritschy JM. Short communication: altered synaptic clustering of GABAA receptors in mice lacking dystrophin (mdx mice). Eur J Neurosci 1999; 11: 4457–62
   PubMed Web of Science ®Google Scholar
• Brunig I, Suter A, Knuesel I, Luscher B, Fritschy JM. GABAergic terminals are required for postsynaptic clustering of dystrophin but not of GABA(A) receptors and gephyrin. J Neurosci 2002; 22: 4805–13
   PubMed Web of Science ®Google Scholar
• Levi S, Grady RM, Henry MD, Campbell KP, Sanes JR, Craig AM. Dystroglycan is selectively associated with inhibitory GABAergic synapses but is dispensable for their differentiation. J Neurosci 2002; 22: 4274–85
   PubMed Web of Science ®Google Scholar
• Kueh SL, Head SI, Morley JW. GABA(A) receptor expression and inhibitory post-synaptic currents in cerebellar Purkinje cells in dystrophin-deficient mdx mice. Clin Exp Pharmacol Physiol 2008; 35: 207–10
   Google Scholar
• Kim TW, Wu K, Xu JL, Black IB. Detection of dystrophin in the postsynaptic density of rat brain and deficiency in a mouse model of Duchenne muscular dystrophy. Proc Natl Acad Sci U S A 1992; 89: 11642–4
   PubMed Web of Science ®Google Scholar
• Peng J, Kim MJ, Cheng D, Duong DM, Gygi SP, Sheng M. Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry. J Biol Chem 2004; 279: 21003–11
   PubMed Web of Science ®Google Scholar
• Mummery R, Sessay A, Lai FA, Beesley PW. Beta-dystroglycan: subcellular localisation in rat brain and detection of a novel immunologically related, postsynaptic density-enriched protein. J Neurochem 1996; 66: 2455–9
   Google Scholar
• Vaillend C, Rendon A, Misslin R, Ungerer A. Influence of dystrophin-gene mutation on mdx mouse behavior. I. Retention deficits at long delays in spontaneous alternation and bar-pressing tasks. Behav Genet 1995; 25: 569–79
   Google Scholar
• Vaillend C, Ungerer A. Behavioral characterization of mdx3cv mice deficient in C-terminal dystrophins. Neuromuscul Disord 1999; 9: 296–304
   PubMed Web of Science ®Google Scholar
• Sesay AK, Errington ML, Levita L, Bliss TV. Spatial learning and hippocampal long-term potentiation are not impaired in mdx mice. Neurosci Lett 1996; 211: 207–10
   PubMed Web of Science ®Google Scholar
• Vaillend C, Billard JM, Laroche S. Impaired long-term spatial and recognition memory and enhanced CA1 hippocampal LTP in the dystrophin-deficient Dmd(mdx) mouse. Neurobiol Dis 2004; 17: 10–20
   PubMed Web of Science ®Google Scholar
• Vaillend C, Billard JM. Facilitated CA1 hippocampal synaptic plasticity in dystrophin-deficient mice: role for GABAA receptors?. Hippocampus 2002; 12: 713–7
   Google Scholar
• Anderson JL, Head SI, Morley JW. Long-term depression is reduced in cerebellar Purkinje cells of dystrophin-deficient mdx mice. Brain Res 2004; 1019: 289–92
   Google Scholar
• Akhavan A, Crivelli SN, Singh M, Lingappa VR, Muschler JL. SEA domain proteolysis determines the functional composition of dystroglycan. FASEB J 2008; 22: 612–21
   Google Scholar
• Esapa CT, Bentham GR, Schroder JE, Kroger S, Blake DJ. The effects of post-translational processing on dystroglycan synthesis and trafficking. FEBS Lett 2003; 555: 209–16
   PubMed Web of Science ®Google Scholar
• Michele DE, Campbell KP. Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J Biol Chem 2003; 278: 15457–60
   PubMed Web of Science ®Google Scholar
• Cohn RD. Dystroglycan: important player in skeletal muscle and beyond. Neuromuscul Disord 2005; 15: 207–17
   PubMedGoogle Scholar
• Williamson RA, Henry MD, Daniels KJ, Hrstka RF, Lee JC, Sunada Y, et al. Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice. Hum Mol Genet 1997; 6: 831–41
   PubMed Web of Science ®Google Scholar
• Moore SA, Saito F, Chen J, Michele DE, Henry MD. Messing A, et al. Deletion of brain dystroglycan recapitulates aspects of congenital muscular dystrophy. Nature 2002; 418: 422–5
   Google Scholar
• Kobayashi K, Nakahori Y, Miyake M, Matsumura K, Kondo-Iida E, Nomura Y, et al. An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy. Nature 1998; 394: 388–92
   PubMed Web of Science ®Google Scholar
• de Bernabe DB, van Bokhoven H, van Beusekom E, Van den Akker W, Kant S, Dobyns WB, et al. A homozygous nonsense mutation in the fukutin gene causes a Walker-Warburg syndrome phenotype. J Med Genet 2003; 40: 845–8
   PubMed Web of Science ®Google Scholar
• Murakami T, Hayashi YK, Noguchi S, Ogawa M, Nonaka I, Tanabe Y, et al. Fukutin gene mutations cause dilated cardiomyopathy with minimal muscle weakness. Ann Neurol 2006; 60: 597–602
   PubMed Web of Science ®Google Scholar
• Godfrey C, Clement E, Mein R, Brockington M, Smith J, Talim B, et al. Refining genotype phenotype correlations in muscular dystrophies with defective glycosylation of dystroglycan. Brain 2007; 130: 2725–35
   PubMed Web of Science ®Google Scholar
• Martin-Rendon E, Blake DJ. Protein glycosylation in disease: new insights into the congenital muscular dystrophies. Trends Pharmacol Sci 2003; 24: 178–83
   Google Scholar
• Martin PT. Congenital muscular dystrophies involving the O-mannose pathway. Curr Mol Med 2007; 7: 417–25
   Google Scholar
• Topaloglu H, Brockington M, Yuva Y, Talim B, Haliloglu G, Blake D, et al. FKRP gene mutations cause congenital muscular dystrophy, mental retardation, and cerebellar cysts. Neurology 2003; 60: 988–92
   Google Scholar
• Aravind L, Koonin EV. The fukutin protein family—predicted enzymes modifying cell-surface molecules. Curr Biol 1999; 9: R836–7
   Google Scholar
• Brockington M, Blake DJ, Prandini P, Brown SC, Torelli S, Benson MA, et al. Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan. Am J Hum Genet 2001; 69: 1198–209
   Google Scholar
• Patnaik SK, Stanley P. Mouse large can modify complex N- and mucin O-glycans on alpha-dystroglycan to induce laminin binding. J Biol Chem 2005; 280: 20851–9
   PubMedGoogle Scholar
• Peyrard M, Seroussi E, Sandberg-Nordqvist AC, Xie YG, Han FY, Fransson I, et al. The human LARGE gene from 22q12.3-q13.1 is a new, distinct member of the glycosyltransferase gene family. Proc Natl Acad Sci U S A 1999; 96: 598–603
   PubMed Web of Science ®Google Scholar
• Barresi R, Michele DE, Kanagawa M, Harper HA, Dovico SA, Satz JS, et al. LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies. Nat Med 2004; 10: 696–703
   Google Scholar
• Philpot J, Cowan F, Pennock J, Sewry C, Dubowitz V, Bydder G, et al. Merosin-deficient congenital muscular dystrophy: the spectrum of brain involvement on magnetic resonance imaging. Neuromuscul Disord 1999; 9: 81–5
   Google Scholar
• Chun SJ, Rasband MN, Sidman RL, Habib AA, Vartanian T. Integrin-linked kinase is required for laminin-2-induced oligodendrocyte cell spreading and CNS myelination. J Cell Biol 2003; 163: 397–408
   PubMedGoogle Scholar
• Holzfeind PJ, Grewal PK, Reitsamer HA, Kechvar J, Lassmann H, Hoeger H, et al. Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle-eye-brain disorders. Hum Mol Genet 2002; 11: 2673–87
   PubMedGoogle Scholar
• Sugita S, Saito F, Tang J, Satz J, Campbell K, Sudhof TC. A stoichiometric complex of neurexins and dystroglycan in brain. J Cell Biol 2001; 154: 435–45
   PubMed Web of Science ®Google Scholar
• Craig AM, Kang Y. Neurexin-neuroligin signaling in synapse development. Curr Opin Neurobiol 2007; 17: 43–52
   PubMed Web of Science ®Google Scholar
• Schroder JE, Tegeler MR, Grosshans U, Porten E, Blank M, Lee J, et al. Dystroglycan regulates structure, proliferation and differentiation of neuroepithelial cells in the developing vertebrate CNS. Dev Biol 2007; 307: 62–78
   Google Scholar
• Blake DJ, Tinsley JM, Davies KE, Knight AE, Winder SJ, Kendrick-Jones J. Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: potentials for protein-protein interactions. Trends Biochem Sci 1995; 20: 133–5
   Google Scholar
• Blake DJ, Nawrotzki R, Loh NY, Gorecki DC, Davies KE. beta-dystrobrevin, a member of the dystrophin-related protein family. Proc Natl Acad Sci U S A 1998; 95: 241–6
   PubMedGoogle Scholar
• Grady RM, Grange RW, Lau KS, Maimone MM, Nichol MC, Stull JT, et al. Role for alpha-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies. Nat Cell Biol 1999; 1: 215–20
   PubMed Web of Science ®Google Scholar
• Loh NY, Nebenius-Oosthuizen D, Blake DJ, Smith AJ, Davies KE. Role of beta-dystrobrevin in nonmuscle dystrophin-associated protein complex-like complexes in kidney and liver. Mol Cell Biol 2001; 21: 7442–8
   PubMedGoogle Scholar
• Grady RM, Wozniak DF, Ohlemiller KK, Sanes JR. Cerebellar synaptic defects and abnormal motor behavior in mice lacking alpha- and beta-dystrobrevin. J Neurosci 2006; 26: 2841–51
   Google Scholar
• Rees ML, Lien CF, Gorecki DC. Dystrobrevins in muscle and non-muscle tissues. Neuromuscul Disord 2007; 17: 123–34
   Web of Science ®Google Scholar
• Benson MA, Sillitoe RV, Blake DJ. Schizophrenia genetics: dysbindin under the microscope. Trends Neurosci 2004; 27: 516–9
   PubMed Web of Science ®Google Scholar
• Burdick KE, Lencz T, Funke B, Finn CT, Szeszko PR, Kane JM, et al. Genetic variation in DTNBP1 influences general cognitive ability. Hum Mol Genet 2006; 15: 1563–8
   PubMed Web of Science ®Google Scholar
• Newell-Litwa K, Seong E, Burmeister M, Faundez V. Neuronal and non-neuronal functions of the AP-3 sorting machinery. J Cell Sci 2007; 120: 531–41
   PubMedGoogle Scholar
• Ahn AH, Yoshida M, Anderson MS, Feener CA, Selig S, Hagiwara Y, et al. Cloning of human basic A1, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8q23-24. Proc Natl Acad Sci U S A 1994; 91: 4446–50
   PubMedGoogle Scholar
• Adams ME, Butler MH, Dwyer TM, Peters MF, Murnane AA, Froehner SC. Two forms of mouse syntrophin, a 58 kd dystrophin-associated protein, differ in primary structure and tissue distribution. Neuron 1993; 11: 531–40
   PubMed Web of Science ®Google Scholar
• Piluso G, Mirabella M, Ricci E, Belsito A, Abbondanza C, Servidei S, et al. Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins localized in neuronal cells. J Biol Chem 2000; 275: 15851–60
   PubMed Web of Science ®Google Scholar
• Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, Santillano DR, et al. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains. Cell 1996; 84: 757–67
   PubMed Web of Science ®Google Scholar
• Adams ME, Kramarcy N, Krall SP, Rossi SG, Rotundo RL, Sealock R, et al. Absence of alpha-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin. J Cell Biol 2000; 150: 1385–98
   PubMed Web of Science ®Google Scholar
• Hosaka Y, Yokota T, Miyagoe-Suzuki Y, Yuasa K, Imamura M, Matsuda R, et al. Alpha1-syntrophin-deficient skeletal muscle exhibits hypertrophy and aberrant formation of neuromuscular junctions during regeneration. J Cell Biol 2002; 158: 1097–107
   PubMed Web of Science ®Google Scholar
• Wertz K, Fuchtbauer EM. Dmd(mdx-beta geo): a new allele for the mouse dystrophin gene. Dev Dyn 1998; 212: 229–41
   Google Scholar
• Haenggi T, Soontornmalai A, Schaub MC, Fritschy JM. The role of utrophin and Dp71 for assembly of different dystrophin-associated protein complexes (DPCs) in the choroid plexus and microvasculature of the brain. Neuroscience 2004; 129: 403–13
   Google Scholar
• Tian M, Jacobson C, Gee SH, Campbell KP, Carbonetto S, Jucker M. Dystroglycan in the cerebellum is a laminin alpha 2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells. Eur J Neurosci 1996; 8: 2739–47
   PubMed Web of Science ®Google Scholar
• Manley GT, Fujimura M, Ma T, Noshita N, Filiz F, Bollen AW, et al. Aquaporin-4 deletion in mice reduces brain edema after acute water intoxication and ischemic stroke. Nat Med 2000; 6: 159–63
   PubMed Web of Science ®Google Scholar
• Amiry-Moghaddam M, Xue R, Haug FM, Neely JD, Bhardwaj A, Agre P, et al. Alpha-syntrophin deletion removes the perivascular but not endothelial pool of aquaporin-4 at the blood-brain barrier and delays the development of brain edema in an experimental model of acute hyponatremia. FASEB J 2004; 18: 542–4
   PubMedGoogle Scholar
• Vajda Z, Pedersen M, Fuchtbauer EM, Wertz K, Stodkilde-Jorgensen H, Sulyok E, et al. Delayed onset of brain edema and mislocalization of aquaporin-4 in dystrophin-null transgenic mice. Proc Natl Acad Sci U S A 2002; 99: 13131–6
   PubMedGoogle Scholar
• Nicchia GP, Rossi A, Nudel U, Svelto M, Frigeri A. Dystrophin-dependent and -independent AQP4 pools are expressed in the mouse brain. Glia 2008; 56: 869–76
   Google Scholar
• Ozawa E, Mizuno Y, Hagiwara Y, Sasaoka T, Yoshida M. Molecular and cell biology of the sarcoglycan complex. Muscle Nerve 2005; 32: 563–76
   PubMedGoogle Scholar
• Zimprich A, Grabowski M, Asmus F, Naumann M, Berg D, Bertram M, et al. Mutations in the gene encoding epsilon-sarcoglycan cause myoclonus-dystonia syndrome. Nat Genet 2001; 29: 66–9
   PubMed Web of Science ®Google Scholar
• Shiga K, Yoshioka H, Matsumiya T, Kimura I, Takeda S, Imamura M. Zeta-sarcoglycan is a functional homologue of gamma-sarcoglycan in the formation of the sarcoglycan complex. Exp Cell Res 2006; 312: 2083–92
   Google Scholar
• Doheny DO, Brin MF, Morrison CE, Smith CJ, Walker RH, Abbasi S, et al. Phenotypic features of myoclonus-dystonia in three kindreds. Neurology 2002; 59: 1187–96
   Google Scholar
• Misbahuddin A, Placzek M, Lennox G, Taanman JW, Warner TT. Myoclonus-dystonia syndrome with severe depression is caused by an exon-skipping mutation in the epsilon-sarcoglycan gene. Mov Disord 2007; 22: 1173–5
   Google Scholar
• Grunewald A, Djarmati A, Lohmann-Hedrich K, Farrell K, Zeller JA, Allert N, et al. Myoclonus-dystonia: significance of large SGCE deletions. Hum Mutat 2008; 29: 331–2
   PubMed Web of Science ®Google Scholar
• Tezenas du Montcel S, Clot F, Vidailhet M, Roze E, Damier P, Jedynak CP, et al. Epsilon sarcoglycan mutations and phenotype in French patients with myoclonic syndromes. J Med Genet 2006; 43: 394–400
   PubMed Web of Science ®Google Scholar
• Esapa CT, Waite A, Locke M, Benson MA, Kraus M, McIlhinney RA, et al. SGCE missense mutations that cause myoclonus-dystonia syndrome impair epsilon-sarcoglycan trafficking to the plasma membrane: modulation by ubiquitination and torsinA. Hum Mol Genet 2007; 16: 327–42
   PubMed Web of Science ®Google Scholar
• Breakefield XO, Blood AJ, Li Y, Hallett M, Hanson PI, Standaert DG. The pathophysiological basis of dystonias. Nat Rev Neurosci 2008; 9: 222–34
   PubMed Web of Science ®Google Scholar
• Chan P, Gonzalez-Maeso J, Ruf F, Bishop DF, Hof PR, Sealfon SC. Epsilon-sarcoglycan immunoreactivity and mRNA expression in mouse brain. J Comp Neurol 2005; 482: 50–73
   Google Scholar
• Nishiyama A, Endo T, Takeda S, Imamura M. Identification and characterization of epsilon-sarcoglycans in the central nervous system. Brain Res Mol Brain Res 2004; 125: 1–12
   PubMedGoogle Scholar
• Ichinose H, Ohye T, Takahashi E, Seki N, Hori T, Segawa M, et al. Hereditary progressive dystonia with marked diurnal fluctuation caused by mutations in the GTP cyclohydrolase I gene. Nat Genet 1994; 8: 236–42
   PubMed Web of Science ®Google Scholar
• Yokoi F, Dang MT, Li J, Li Y. Myoclonus, motor deficits, alterations in emotional responses and monoamine metabolism in epsilon-sarcoglycan deficient mice. J Biochem 2006; 140: 141–6
   Google Scholar
• Draviam RA, Shand SH, Watkins SC. The beta-delta-core of sarcoglycan is essential for deposition at the plasma membrane. Muscle Nerve 2006; 34: 691–701
   PubMed Web of Science ®Google Scholar
• Allikian MJ, McNally EM. Processing and assembly of the dystrophin glycoprotein complex. Traffic 2007; 8: 177–83
   Google Scholar
• Chan YM, Bonnemann CG, Lidov HG, Kunkel LM. Molecular organization of sarcoglycan complex in mouse myotubes in culture. J Cell Biol 1998; 143: 2033–44
   PubMed Web of Science ®Google Scholar
• Cai H, Erdman RA, Zweier L, Chen J, Shaw JH 4th, Baylor KA, et al. The sarcoglycan complex in Schwann cells and its role in myelin stability. Exp Neurol 2007; 205: 257–69
   Google Scholar
• Durbeej M, Cohn RD, Hrstka RF, Moore SA, Allamand V, Davidson BL, et al. Disruption of the beta-sarcoglycan gene reveals pathogenetic complexity of limb-girdle muscular dystrophy type 2E. Mol Cell 2000; 5: 141–51
   PubMed Web of Science ®Google Scholar
• Sakamoto A, Ono K, Abe M, Jasmin G, Eki T, Murakami Y, et al. Both hypertrophic and dilated cardiomyopathies are caused by mutation of the same gene, delta-sarcoglycan, in hamster: an animal model of disrupted dystrophin-associated glycoprotein complex. Proc Natl Acad Sci U S A 1997; 94: 13873–8
   PubMed Web of Science ®Google Scholar
• Hjermind LE, Vissing J, Asmus F, Krag T, Lochmuller H, Walter MC, et al. No muscle involvement in myoclonus-dystonia caused by epsilon-sarcoglycan gene mutations. Eur J Neurol 2008; 15: 525–9
   Google Scholar
• Draviam RA, Wang B, Shand SH, Xiao X, Watkins SC. Alpha-sarcoglycan is recycled from the plasma membrane in the absence of sarcoglycan complex assembly. Traffic 2006; 7: 793–810
   PubMed Web of Science ®Google Scholar
• Breitkreutz BJ, Stark C, Tyers M. Osprey: a network visualization system. Genome Biol 2003; 4: R22
   PubMed Web of Science ®Google Scholar
• Bresolin N, Castelli E, Comi GP, Felisari G, Bardoni A, Perani D, et al. Cognitive impairment in Duchenne muscular dystrophy. Neuromuscul Disord 1994; 4: 359–69
   PubMed Web of Science ®Google Scholar
• Hinton VJ, De Vivo DC, Fee R, Goldstein E, Stern Y. Investigation of poor academic achievement in children with Duchenne muscular dystrophy. Learn Disabil Res Pract 2004; 19: 146–54
   PubMedGoogle Scholar
• Young HK, Barton BA, Waisbren S, Portales Dale L, Ryan MM, Webster RI, et al. Cognitive and psychological profile of males with Becker muscular dystrophy. J Child Neurol 2008; 23: 155–62
   PubMedGoogle Scholar
• Wu JY, Kuban KC, Allred E, Shapiro F, Darras BT. Association of Duchenne muscular dystrophy with autism spectrum disorder. J Child Neurol 2005; 20: 790–5
   PubMedGoogle Scholar
• Okumura A, Nagai K, Okumura N. Interaction of alpha1-syntrophin with multiple isoforms of heterotrimeric G protein alpha subunits. FEBS J 2008; 275: 22–33
   Google Scholar
• Yamakawa H, Oyama S, Mitsuhashi H, Sasagawa N, Uchino S, Kohsaka S, et al. Neuroligins 3 and 4X interact with syntrophin-gamma2, and the interactions are affected by autism-related mutations. Biochem Biophys Res Commun 2007; 355: 41–6
   Google Scholar
• Garcia RA, Vasudevan K, Buonanno A. The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses. Proc Natl Acad Sci U S A 2000; 97: 3596–601
   PubMedGoogle Scholar
• Vandebrouck A, Sabourin J, Rivet J, Balghi H, Sebille S, Kitzis A, et al. Regulation of capacitative calcium entries by alpha1-syntrophin: association of TRPC1 with dystrophin complex and the PDZ domain of alpha1-syntrophin. FASEB J 2007; 21: 608–17
   Google Scholar
• Chen Z, Hague C, Hall RA, Minneman KP. Syntrophins regulate alpha1D-adrenergic receptors through a PDZ domain-mediated interaction. J Biol Chem 2006; 281: 12414–20
   PubMed Web of Science ®Google Scholar
• Buechler C, Boettcher A, Bared SM, Probst MC, Schmitz G. The carboxyterminus of the ATP-binding cassette transporter A1 interacts with a beta2-syntrophin/utrophin complex. Biochem Biophys Res Commun 2002; 293: 759–65
   PubMed Web of Science ®Google Scholar
• Hogan A, Yakubchyk Y, Chabot J, Obagi C, Daher E, Maekawa K, et al. The phosphoinositol 3,4-bisphosphate-binding protein TAPP1 interacts with syntrophins and regulates actin cytoskeletal organization. J Biol Chem 2004; 279: 53717–24
   Google Scholar
• Hogan A, Shepherd L, Chabot J, Quenneville S, Prescott SM, Topham MK, et al. Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions. J Biol Chem 2001; 276: 26526–33
   PubMed Web of Science ®Google Scholar
• Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, et al. Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins. J Biol Chem 2004; 279: 22331–46
   PubMed Web of Science ®Google Scholar
• Connors NC, Adams ME, Froehner SC, Kofuji P. The potassium channel Kir4.1 associates with the dystrophin-glycoprotein complex via alpha-syntrophin in glia. J Biol Chem 2004; 279: 28387–92
   PubMedGoogle Scholar
• Neely JD, Amiry-Moghaddam M, Ottersen OP, Froehner SC, Agre P, Adams ME. Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein. Proc Natl Acad Sci U S A 2001; 98: 14108–13
   PubMed Web of Science ®Google Scholar
• Lumeng C, Phelps S, Crawford GE, Walden PD, Barald K, Chamberlain JS. Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases. Nat Neurosci 1999; 2: 611–7
   PubMed Web of Science ®Google Scholar
• Hasegawa M, Cuenda A, Spillantini MG, Thomas GM, Buee-Scherrer V, Cohen P, et al. Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition. J Biol Chem 1999; 274: 12626–31
   PubMedGoogle Scholar
• Gee SH, Madhavan R, Levinson SR, Caldwell JH, Sealock R, Froehner SC. Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins. J Neurosci 1998; 18: 128–37
   PubMed Web of Science ®Google Scholar
• Williams JC, Armesilla AL, Mohamed TM, Hagarty CL, McIntyre FH, Schomburg S, et al. The sarcolemmal calcium pump, alpha-1 syntrophin, and neuronal nitric-oxide synthase are parts of a macromolecular protein complex. J Biol Chem 2006; 281: 23341–8
   PubMed Web of Science ®Google Scholar
• Iwata Y, Pan Y, Yoshida T, Hanada H, Shigekawa M. Alpha1-syntrophin has distinct binding sites for actin and calmodulin. FEBS Lett 1998; 423: 173–7
   PubMedGoogle Scholar
• Newbell BJ, Anderson JT, Jarrett HW. Ca2 + -calmodulin binding to mouse alpha1 syntrophin: syntrophin is also a Ca2 + -binding protein. Biochemistry 1997; 36: 1295–305
   PubMed Web of Science ®Google Scholar
• Olalla L, Aledo JC, Bannenberg G, Marquez J. The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins. FEBS Lett 2001; 488: 116–22
   Google Scholar