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1
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0017598654
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The distribution of alpha-bungarotoxin binding sites on mammalian muscle developing in vivo
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(1977)
J Physiol
, vol.267
, pp. 195-213
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Bevan1
Steinbach2
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6
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0027723681
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Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons
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of special interest, By inhibiting expression of gephyrin, a glycine receptor associated protein, the authors demonstrate that gephyrin is necessary for the formation of glycine receptor clusters in the dendritic plasma membrane of rat spinal neurons in culture. This is the first intracellular protein other than rapsyn that has been shown to play a direct role in clustering of neurotransmitter receptors.
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(1993)
Nature
, vol.366
, pp. 745-748
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Kirsch1
Wolters2
Triller3
Betz4
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8
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0027273473
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The distribution of glutamate receptors in cultured rat hippocampal neurons: postsynaptic clustering of AMPA-selective subunits
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(1993)
Neuron
, vol.10
, pp. 1055-1068
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Craig1
Blackstone2
Huganir3
Banker4
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9
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0026000830
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The submembrane machinery for nicotinic acetylcholine receptor clustering
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(1991)
J Cell Biol
, vol.114
, pp. 1-7
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Froehner1
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12
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0027368111
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Clustering and immobilization of acetylcholine receptors by the 43-kD protein: a possible role for dystrophin-related protein
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of outstanding interest, Overexpression of rapsyn by transfection into a muscle cell line caused a dramatic difference in the size of the AChR clusters formed, and, interestingly, utrophin (dystrophin-related protein) was shown to co-localize with the large clusters formed in non-transfected cells but not with the smaller clusters in cells overexpressing rapsyn. These results provide the first indication that utrophin may be principally involved in the enlargement of AChR clusters.
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(1993)
J Cell Biol
, vol.123
, pp. 729-740
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Phillips1
Noakes2
Roberds3
Campbell4
Merlie5
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14
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0027481757
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The 87K postsynaptic membrane protein from Torpedo is a protein-tyrosine kinase substrate homologous to dystrophin
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of special interest, Cloning of the cDNA that encodes the Torpedo 87 kDa postsynaptic membrane protein revealed that the predicted protein sequence is homologous to the carboxy-terminal domains of dystrophin. Tissue distribution of the 87 kDa mRNA was examined, and phosphorylation of 87 kDa on multiple residues was demonstrated. Co-immunoprecipitation experiments demonstrated that 87 kDa associates with syntrophin and dystrophin.
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(1993)
Neuron
, vol.10
, pp. 511-522
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Wagner1
Cohen2
Huganir3
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15
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0026611958
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Association of the Mr 58,000 postsynaptic protein of electric tissue with Torpedo dystrophin and the Mr 87,000 postsynaptic protein
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(1992)
J Biol Chem
, vol.267
, pp. 6213-6218
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Butler1
Douville2
Murnane3
Kramarcy4
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16
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0028145301
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Association of utrophin and multiple dystrophin short forms with the mammalian M(r) 58,000 dystrophin-associated protein (syntrophin)
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of special interest, By identifying species that co-purify in immunoaffinity purifications from rat tissues, the authors demonstrate interactions between syntrophin, dystrophin, utrophin and 87 kDa. This study extends previous results from similar experiments carried out with extracts from Torpedo [14,15]. Together these studies present compelling biochemical evidence suggesting that syntrophin, dystrophin/utrophin and 87 kDa exist in a complex.
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(1994)
J Biol Chem
, vol.269
, pp. 2870-2876
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Kramarcy1
Vidal2
Froehner3
Sealock4
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17
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0028206868
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Molecular organization at the glycoprotein-complex-binding site of dystrophin. Three dystrophin-associated proteins bind directly to the carboxy-terminal portion of dystrophin
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of special interest, Using a gel overlay approach, dystrophin was shown to interact directly with β-dystroglycan, syntrophin and 87 kDa. In addition, the binding domain for each of these interacting proteins on dystrophin was mapped. This report is the first to establish that dystrophin associates with the dystrophin-associated glycoprotein complex via interactions with β-dystroglycan.
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(1994)
Eur J Biochem
, vol.220
, pp. 283-292
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Suzuki1
Yoshida2
Hayashi3
Mizuno4
Hagiwara5
Ozawa6
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18
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0027375539
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Two forms of mouse syntrophin, a 58 kD dystrophin-associated protein, differ in primary structure and tissue distribution
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of special interest, of outstanding interest, See annotation to [20].
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(1993)
Neuron
, vol.11
, pp. 531-540
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Adams1
Butler2
Dwyer3
Peters4
Murnane5
Froehner6
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19
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0027998866
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Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression
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of special interest, of outstanding interest, See annotation to [20].
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(1994)
J Biol Chem
, vol.269
, pp. 6040-6044
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Yang1
Ibraghimov2
Moomaw3
Slaughter4
Campbell5
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20
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0028219584
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Cloning of human basic A1, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8q23-24
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of outstanding interest, of special interest, Studies presented in [18,19,20] describe the isolation and characterization of syntrophin cDNAs, revealing a multigene family of syntrophin proteins. The first reports of cDNA sequences appear in [18,19], and human syntrophin sequences are reported in [20]. The different syntrophins display distinct tissue distributions, and, interestingly, syntrophin-1 expression parallels that of dystrophin, whereas syntrophin-2 is found in the same tissues as utrophin. See also [21].
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 4446-4450
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Ahn1
Yoshida2
Anderson3
Feener4
Selig5
Hagiwara6
Ozawa7
Kunkel8
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21
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0027935193
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Beta-2-syntrophin — localization at the neuromuscular junction in skeletal muscle
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of special interest, of outstanding interest, Antibodies specific for syntrophin-2 (β2-syntrophin) labeled only the neuromuscular junction in rat skeletal muscle, whereas syntrophin-1 was detected at both the neuromuscular junction and throughout the sarcolemma. Coupled with results from tissue distribution studies described in [18,19,20], these intriguing observations strongly suggest that syntrophin-2 may interact specifically with utrophin at synaptic clusters of AChRs, and, therefore, may be the most relevant syntrophin isoform with regard to assembly of the postsynaptic apparatus.
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(1994)
Neuroreport
, vol.5
, pp. 1577-1580
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Peters1
Kramarcy2
Sealock3
Froehner4
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23
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0028321841
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Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: a heteromeric complex related to the dystroglycans
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of outstanding interest, See annotation to [26].
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(1994)
Neuron
, vol.12
, pp. 1173-1180
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Bowe1
Deyst2
Leszyk3
Fallon4
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24
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0028306787
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A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering
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of outstanding interest, See annotation to [26].
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(1994)
Cell
, vol.77
, pp. 663-674
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Campanelli1
Roberds2
Campbell3
Scheller4
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25
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0028178082
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Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor
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of outstanding interest, See annotation to [26].
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(1994)
Cell
, vol.77
, pp. 675-686
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Gee1
Montanaro2
Lindenbaum3
Carbonetto4
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26
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0027941192
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Dystroglycan binds nerve and muscle agrin
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of outstanding interest, Four separate groups [23–26] reported the identification of an agrin-binding protein as α-dystroglycan, the extracellular component of the dystrophin-associated glycoprotein complex. This discovery establishes for the first time a possible link between the extracellular binding of agrin and the intracellular events that mediate formation of AChR clusters. Although the evidence for agrin binding to α-dystroglycan is sound, it remains to be unambiguously determined whether α-dystroglycan is a functional agrin receptor that is necessary for transducing the agrin signal for AChR clustering.
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(1994)
Neuron
, vol.13
, pp. 103-115
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Sugiyama1
Bowen2
Hall3
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28
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0025242185
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Glycoprotein complex anchoring dystrophin to sarcolemma
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(1990)
J Biochem
, vol.108
, pp. 748-752
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Yoshida1
Ozawa2
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29
-
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0028047235
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Dystrophin-glycoprotein complex: Its role in the molecular pathogenesis of muscular dystrophies
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(1994)
Muscle & Nerve
, vol.17
, pp. 2-15
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Matsumura1
Campbell2
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30
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0025815479
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Membrane organization of the dystrophin—glycoprotein complex
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of special interest, A model of the dystrophin-associated glycoprotein complex (DGC) complex is proposed based on several biochemical and structural properties of the DGC complex components. Dystrophin and syntrophin (59 kDa) are demonstrated to be cytoskeletal elements that are tightly linked to an integral membrane complex composed of a 25 kDa protein, 50 kDa (adhalin), 43 kDa (β-dystroglycan) and 35 kDa sarcolemmal glycoproteins, and an extracellular glycoprotein of 156 kDa (α-dystroglycan). These elegant experiments have paved the way for subsequent studies probing the structure and function of the DGC.
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(1991)
Cell
, vol.66
, pp. 1121-1131
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Ervasti1
Campbell2
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33
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0028260234
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Staurosporine inhibits agrin-induced acetylcholine receptor phosphorylation and aggregation
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(1994)
J Cell Biol
, vol.125
, pp. 661-668
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Wallace1
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34
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0026684767
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Mechanism of agrin-induced acetylcholine receptor aggregation
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(1992)
J Neurobiol
, vol.23
, pp. 592-604
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Wallace1
-
35
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0027363678
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Molecular cloning of two abundant protein tyrosine kinases in Torpedo electric organ that associate with the acetylcholine receptor
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(1993)
J Biol Chem
, vol.268
, pp. 25152-25161
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Swope1
Huganir2
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