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Volumn 14, Issue 1, 2013, Pages 87-94

Nicotinamide mononucleotide adenylyltransferase maintains active zone structure by stabilizing Bruchpilot

Author keywords

active zone; BRP; chaperone; NMNAT; protein homeostasis

Indexed keywords

BRUCHPILOT PROTEIN; MEMBRANE PROTEIN; NICOTINAMIDE NUCLEOTIDE ADENYLYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84871918972     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2012.181     Document Type: Article
Times cited : (19)

References (23)
  • 1
    • 33646724067 scopus 로고    scopus 로고
    • Bruchpilot promotes active zone assembly, Ca2\+ channel clustering, and vesicle release
    • Kittel RJ et al (2006) Bruchpilot promotes active zone assembly, Ca2\+ channel clustering, and vesicle release. Science 312: 1051-1054
    • (2006) Science , vol.312 , pp. 1051-1054
    • Kittel, R.J.1
  • 2
    • 33748940272 scopus 로고    scopus 로고
    • Molecular organization of the presynaptic active zone
    • DOI 10.1007/s00441-006-0244-y
    • Schoch S, Gundelfinger ED (2006) Molecular organization of the presynaptic active zone. Cell Tissue Res 326: 379-391 (Pubitemid 44435815)
    • (2006) Cell and Tissue Research , vol.326 , Issue.2 , pp. 379-391
    • Schoch, S.1    Gundelfinger, E.D.2
  • 3
    • 8144230701 scopus 로고    scopus 로고
    • The architecture of the active zone in the presynaptic nerve terminal
    • Zhai RG, Bellen HJ (2004) The architecture of the active zone in the presynaptic nerve terminal. Physiology 19: 262-270 (Pubitemid 39472637)
    • (2004) Physiology , Issue.5 , pp. 262-270
    • Zhai, R.G.1    Bellen, H.J.2
  • 4
    • 0028879136 scopus 로고
    • Cysteine string protein, a DnaJ family member, is present on diverse secretory vesicles
    • Braun JE, Scheller RH (1995) Cysteine string protein, a DnaJ family member, is present on diverse secretory vesicles. Neuropharmacology 34: 1361-1369
    • (1995) Neuropharmacology , vol.34 , pp. 1361-1369
    • Braun, J.E.1    Scheller, R.H.2
  • 5
    • 0031149356 scopus 로고    scopus 로고
    • The DnaJ-like cysteine string protein and exocytotic neurotransmitter release
    • DOI 10.1016/S0166-2236(96)10082-5, PII S0166223696100825
    • Buchner E, Gundersen CB (1997) The DnaJ-like cysteine string protein and exocytotic neurotransmitter release. Trends Neurosci 20: 223-227 (Pubitemid 27158052)
    • (1997) Trends in Neurosciences , vol.20 , Issue.5 , pp. 223-227
    • Buchner, E.1    Gundersen, C.2
  • 6
    • 0034652087 scopus 로고    scopus 로고
    • Comparison of cysteine string protein (Csp) and mutant α-SNAP overexpression reveals a role for Csp in late steps of membrane fusion in dense-core granule exocytosis in adrenal chromaffin cells
    • Graham ME, Burgoyne RD (2000) Comparison of cysteine string protein (Csp) and mutant alpha-SNAP overexpression reveals a role for csp in late steps of membrane fusion in dense-core granule exocytosis in adrenal chromaffin cells. J Neurosci 20: 1281-1289 (Pubitemid 30220406)
    • (2000) Journal of Neuroscience , vol.20 , Issue.4 , pp. 1281-1289
    • Graham, M.E.1    Burgoyne, R.D.2
  • 7
    • 54049132555 scopus 로고    scopus 로고
    • Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein
    • Greaves J, Salaun C, Fukata Y, Fukata M, Chamberlain LH (2008) Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein. J Biol Chem 283: 25014-25026
    • (2008) J Biol Chem , vol.283 , pp. 25014-25026
    • Greaves, J.1    Salaun, C.2    Fukata, Y.3    Fukata, M.4    Chamberlain, L.H.5
  • 9
    • 42249103603 scopus 로고    scopus 로고
    • NAD synthase NMNAT acts as a chaperone to protect against neurodegeneration
    • DOI 10.1038/nature06721, PII NATURE06721
    • Zhai RG, Zhang F, Hiesinger PR, Cao Y, Haueter CM, Bellen HJ (2008) NAD synthase NMNAT acts as a chaperone to protect against neurodegeneration. Nature 452: 887-891 (Pubitemid 351550857)
    • (2008) Nature , vol.452 , Issue.7189 , pp. 887-891
    • Zhai, R.G.1    Zhang, F.2    Hiesinger, P.R.3    Cao, Y.4    Haueter, C.M.5    Bellen, H.J.6
  • 12
    • 84988044061 scopus 로고    scopus 로고
    • A protocol for mosaic analysis with a repressible cell marker (MARCM) in Drosophila
    • Wu JS, Luo L (2006) A protocol for mosaic analysis with a repressible cell marker (MARCM) in Drosophila. Nat Protoc 1: 2583-2589
    • (2006) Nat Protoc , vol.1 , pp. 2583-2589
    • Wu, J.S.1    Luo, L.2
  • 13
    • 49549119765 scopus 로고    scopus 로고
    • Roles of ubiquitination at the synapse
    • Haas KF, Broadie K (2008) Roles of ubiquitination at the synapse. Biochim Biophys Acta 1779: 495-506
    • (2008) Biochim Biophys Acta , vol.1779 , pp. 495-506
    • Haas, K.F.1    Broadie, K.2
  • 14
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • DOI 10.1038/502
    • Cummings CJ, Mancini MA, Antalffy B, DeFranco DB, Orr HT, Zoghbi HY (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet 19: 148-154 (Pubitemid 28248795)
    • (1998) Nature Genetics , vol.19 , Issue.2 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 15
    • 77957798838 scopus 로고    scopus 로고
    • Hsp70-and Hsp90-mediated proteasomal degradation underlies TPI sugarkill pathogenesis in Drosophila
    • Hrizo SL, Palladino MJ (2010) Hsp70-and Hsp90-mediated proteasomal degradation underlies TPI sugarkill pathogenesis in Drosophila. Neurobiol Dis 40: 676-683
    • (2010) Neurobiol Dis , vol.40 , pp. 676-683
    • Hrizo, S.L.1    Palladino, M.J.2
  • 16
    • 64249122538 scopus 로고    scopus 로고
    • Widespread changes in synaptic markers as a function of sleep and wakefulness in Drosophila
    • Gilestro GF, Tononi G, Cirelli C (2009) Widespread changes in synaptic markers as a function of sleep and wakefulness in Drosophila. Science 324: 109-112
    • (2009) Science , vol.324 , pp. 109-112
    • Gilestro, G.F.1    Tononi, G.2    Cirelli, C.3
  • 18
    • 77952729399 scopus 로고    scopus 로고
    • Rapid structural alterations of the active zone lead to sustained changes in neurotransmitter release
    • Matz J, Gilyan A, Kolar A, McCarvill T, Krueger SR (2010) Rapid structural alterations of the active zone lead to sustained changes in neurotransmitter release. Proc Natl Acad Sci USA 107: 8836-8841
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 8836-8841
    • Matz, J.1    Gilyan, A.2    Kolar, A.3    McCarvill, T.4    Krueger, S.R.5
  • 19
    • 33746445842 scopus 로고    scopus 로고
    • Activity-related redistribution of presynaptic proteins at the active zone
    • Tao-Cheng JH (2006) Activity-related redistribution of presynaptic proteins at the active zone. Neuroscience 141: 1217-1224
    • (2006) Neuroscience , vol.141 , pp. 1217-1224
    • Tao-Cheng, J.H.1
  • 23
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • DOI 10.1038/nn1013
    • Ehlers MD (2003) Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nat Neurosci 6: 231-242 (Pubitemid 36278281)
    • (2003) Nature Neuroscience , vol.6 , Issue.3 , pp. 231-242
    • Ehlers, M.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.