Targeting acetylcholinesterase to the neuromuscular synapse

Chemico-Biological Interactions

Volumn 157-158, Issue , 2005, Pages 15-21

  Rotundo, Richard L ^a,b   Rossi, Susana G ^a   Kimbell, Lewis M ^a   Ruiz, Carlos ^a   Marrero, Emilio ^a  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

^b Neuroscience Program   (United States)

Author keywords

Collagenic tail; Muscle; Nerve; Protein biogenesis; Protein targeting; Synaptogenesis

Indexed keywords

ACETYLCHOLINESTERASE; AGRIN; BREFELDIN A; CHOLINERGIC RECEPTOR; COLLAGEN; DYSTROGLYCAN; ENZYME; LAMININ; MUSK RECEPTOR; PERLACAN; PROTEIN; PROTEOHEPARAN SULFATE; RAPSYN; TETRAMER; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG;

BASEMENT MEMBRANE; BINDING SITE; CELL NUCLEUS; CELL SURFACE; CELL TRANSPORT; CONFERENCE PAPER; ENZYME ACTIVE SITE; ENZYME LOCALIZATION; ENZYME SYNTHESIS; GENE TRANSLOCATION; GENETIC TRANSCRIPTION; GOLGI COMPLEX; IMMUNOPRECIPITATION; IN VIVO STUDY; INTRACELLULAR SPACE; MICROTITER PLATE ASSAY; MOLECULAR MODEL; MUSCLE; MUSCLE FIBER MEMBRANE; MYOTUBE; NEUROMUSCULAR SYNAPSE; NONHUMAN; PROTEIN BINDING; PROTEIN TARGETING; QUAIL; ROUGH ENDOPLASMIC RETICULUM; SOLID; SYNAPSE;

ACETYLCHOLINESTERASE; ANIMALS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GOLGI APPARATUS; HEPARAN SULFATE PROTEOGLYCANS; HUMANS; MULTIGENE FAMILY; NEUROMUSCULAR JUNCTION; PROTEIN BINDING; SYNAPSES;

PHASIANIDAE;

EID: 28744433406     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2005.10.007     Document Type: Conference Paper

References (45)

1. C. Legay Why so many forms of acetylcholinesterase? Microsc. Res. Tech. 49 2000 56 72
2. R.L. Rotundo Expression and localization of acetylcholinesterase at the neuromuscular junction J. Neurocytol. 32 2003 743 766
3. R. Aldunate, J.C. Casar, E. Brandan, and N.C. Inestrosa Structural and functional organization of synaptic acetylcholinesterase Brain Res. Brain Res. Rev. 47 2004 96 104
4. Z.W. Hall, and R.B. Kelly Enzymatic detachment of endplate acetylcholinesterase from muscle Nature 232 1979 62 63
5. U.J. McMahan, J.R. Sanes, and L.M. Marshall Cholinesterase is associated with the basal lamina at the neuromuscular junction Nature 271 1978 172 174
6. S.G. Rossi, and R.L. Rotundo Localization of "non-extractable" acetylcholinesterase to the vertebrate neuromuscular junction J. Biol. Chem. 1993
7. J.S. Lwebuga-Mukasa, S. Lappi, and P. Taylor Molecular forms of acetylcholinesterase from Torpedo californica: their relationship to synaptic membranes Biochemistry 15 1976 1425 1434
8. S. Bon, J. Cartaud, and J. Massoulie The dependence of acetylcholinesterase aggregation at low ionic strength upon a polyanionic component Eur. J. Biochem. 85 1978 1 14
9. E. Brandan, and N.C. Inestrosa Binding of the asymmetric forms of acetylcholinesterase to heparin Biochem. J. 221 1984 415 422
10. R.L. Rotundo, S.G. Rossi, and L. Anglister Transplantation of quail collagen-tailed acetylcholinesterase molecules onto the frog neuromuscular synapse J. Cell Biol. 136 1997 367 374
11. G. Feng, E. Krejci, J. Molgo, J.M. Cunningham, J. Massoulie, and J.R. Sanes Genetic analysis of collagen Q: roles in acetylcholinesterase and butyrylcholinesterase assembly and in synaptic structure and function J. Cell Biol. 144 1999 1349 1360
12. E. Arikawa-Hirasawa, S.G. Rossi, R.L. Rotundo, and Y. Yamada Absence of acetylcholinesterase at the neuromuscular junctions of perlecan-null mice Nat. Neurosci. 5 2002 119 123
13. C. Jacobson, P.D. Cote, S.G. Rossi, R.L. Rotundo, and S. Carbonetto The dystroglycan complex is necessary for stabilization of acetylcholine receptor clusters at neuromuscular junctions and formation of the synaptic basement membrane J. Cell Biol. 152 2001 435 450
14. H.B. Peng, H. Xie, S.G. Rossi, and R.L. Rotundo Acetylcholinesterase clustering at the neuromuscular junction involves perlecan and dystroglycan J. Cell Biol. 145 1999 911 921
15. J. Massoulie, L. Pezzementi, S. Bon, E. Krejci, and F.M. Valette Molecular and cellular biology of cholinesterases Prog. Neurobiol. 41 1993 31 91
16. R.L. Rotundo, and A.M. Gomez Nucleus-specific translation and assembly of acetylcholinesterase in multinucleated muscle cells J. Cell Biol. 110 1990
17. S.G. Rossi, and R.L. Rotundo Cell surface acetylcholinesterase molecules on multinucleated myotubes are clustered over the nucleus of origin J. Cell Biol. 119 1992 1657 1667
18. B.J. Jasmin, R.K. Lee, and R.L. Rotundo Compartmentalization of acetylcholinesterase mRNA and enzyme at the vertebrate neuromuscular junction Neuron 11 1993 467 477
19. R.N. Michel, C.Q. Vu, W. Tetzlaff, and B.J. Jasmin Neural regulation of acetylcholinesterase mRNAs at mammalian neuromuscular synapses J. Cell Biol. 127 1994 1061 1069
20. C. Legay, M. Huchet, J. Massoulie, and J.-P. Changeux Developmental regulation of acetylcholinesterase transcripts in the mouse diaphragm: alternative splicing and focalization Eur. J. Neurosci. 7 1995 1803 1809
21. S.G. Rossi, and R.L. Rotundo Transient interactions between collagen-tailed acetylcholinesterase and sulfated proteoglycans prior to immobilization on the extracellular matrix J. Biol. Chem. 271 1996 1979 1987
22. M. Vigny, G.R. Martin, and G.R. Grotendorst Interactions of asymmetric forms of acetylcholinesterase with basement membrane components J. Biol. Chem. 258 1983 8794 8798
23. M.J. Anderson, and D.M. Fambrough Aggregates of acetylcholine receptors are associated with plaques of a basal lamina heparan sulfate proteoglycan on the surface of skeletal muscle fibers J. Cell Biol. 97 1983 1396 1411
24. E.K. Bayne, M.J. Anderson, and D.M. Fambrough Extracellular matrix organization in developing muscle: correlation with acetylcholine receptor aggregates J. Cell Biol. 99 1984 1486 1501
25. M.J. Anderson, F.G. Klier, and K.E. Tanguay Acetylcholine receptor aggregation parallels the deposition of a basal lamina proteoglycan during development of the neuromuscular junction J. Cell Biol. 99 1984 1769 1784
26. J.C. Torres, M.I. Behrens, and N.C. Inestrosa Neural 16S acetylcholinesterase is solubilized by heparin Biochem. J. 215 1983 201 204
27. A. Barat, E. Escudero, and G. Ramirez Heparin and the solubilization of asymmetric acetylcholinesterase FEBS Lett. 195 1986 209 214
28. H.B. Peng, A.A. Ali, D.F. Daggett, H. Rauvala, J.R. Hassell, and N.R. Smalheiser The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction Cell Adhes. Commun. 5 1998 475 489
29. E. Hohenester, D. Tisi, J.F. Talts, and R. Timpl The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin Mol. Cell 4 1999 783 792
30. L.M. Kimbell, K. Ohno, A.G. Engel, and R.L. Rotundo C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse J. Biol. Chem. 279 2004 10997 11005
31. S.G. Rossi, A.E. Vazquez, and R.L. Rotundo Local control of acetylcholinesterase gene expression in multinucleated skeletal muscle fibers: individual nuclei respond to signals from the overlying plasma membrane J. Neurosci. 20 3 2000 919 928
32. G. Tsen, W. Halfter, S. Kroger, and G.J. Cole Agrin is a heparan sulfate proteglycan J. Biol. Chem. 270 7 1995 3392 3399
33. A. Cartaud, L. Strochlic, M. Guerra, B. Blanchard, M. Lambergeon, E. Krejci, J. Cartaud, and C. Legay MuSK is required for anchoring acetylcholinesterase at the neuromuscular junction J. Cell Biol. 165 2004 505 515
34. M. Gautam, P.G. Noakes, L. Moscoso, F. Rupp, R.H. Scheller, J.P. Merlie, and J.R. Sanes Defective neuromuscular synaptogensis in agrin-deficient mutant mice Cell 85 1996 525 535
35. E.D. Apel, D.J. Glass, L.M. Moscoso, G.D. Yancopoulos, and J.R. Sanes Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold Neuron 18 1997 623 635
36. A.G. Engel, E.H. Lambert, and M.R. Gomez A new myasthenic syndrome with end-plate acetylcholinesterase deficiency, small nerve terminals, and reduced acetylcholine release Ann. Neurol. 1 1977 315 330
37. S. Camp, S. Bon, Y. Li, D.K. Getman, A.G. Engel, J. Massoulie, and P. Taylor Patients with congenital myasthenia associated with end-plate acetylcholinesterase deficiency show normal sequence, mRNA splicing, and assembly of catalytic subunits J. Clin. Invest. 95 1995 333 340
38. K. Ohno, J. Brengman, A. Tsujino, and A.G. Engel Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme Proc. Natl. Acad. Sci. U.S.A. 95 1998 9654 9659
39. C. Donger, E. Krejci, A.P. Serradell, B. Eymard, S. Bon, S. Nicole, D. Chateau, F. Gary, M. Fardeau, J. Massoulie, and P. Guicheney Mutation in the human acetylcholinesterase-associated collagen gene, COLQ is responsibe for congenital myasthenic syndrome with end-plate acetylcholinesterase dieficiency (type Ic) Am. J. Hum. Genet. 1998
40. K. Ohno, J. Brengman, K.J. Felice, D.R. Cornblath, and A.G. Engel Congenital end-plate acetylcholinesterase deficiency caused by a nonsense mutation and an A to G splice donor site mutation at position +3 of the collagenlike tail subunit gene (COLQ): how does G at position +3 result in abberant splicing? Am. J. Hum. Genet. 65 1999 635 644
41. K. Ohno, A.G. Engel, J. Brengman, X. Shen, F. Heidenreich, A. Vincent, M. Milone, E. Tan, M. Demirci, P. Walsh, S. Nakano, and I. Akiguchi The spectrum of mutations causing end-plate acetylcholinesterase deficiency Ann. Neurol. 47 2000 162 170
42. P. Deprez, N.C. Inestrosa, and E. Krejci Two different heparin-binding domains in the triple-helical domain of ColQ, the collagen tail subunit of synaptic acetylcholinesterase J. Biol. Chem. 2003
43. P.N. Deprez, and N.C. Inestrosa Two heparin-binding domains are present on the collagenic tail of asymmetric acetylcholinesterase J. Biol. Chem. 270 12 1995 11043 11046
44. R.L. Rotundo Asymmetric acetylcholinesterase is assembled in the golgi apparatus Proc. Natl. Acad. Sci. U.S.A. 81 1984 479 483
45. H. Kasprzak, and M.M. Salpeter Recovery of acetylcholinesterase at intact neuromuscular junctions after in vivo inactivation with Di- isopropylfluorophoosphate J. Neurosc. 5 1985 951 955