메뉴 건너뛰기




Volumn 288, Issue 11, 2013, Pages 7438-7449

Erratum: a-Synuclein membrane association is regulated by the Rab3a recycling machinery and presynaptic activity (Journal of Biological Chemistry (2013) 288 (7438-7449) DOI: 10.1074/jbc.M112.439497);α-Synuclein membrane association is regulated by the Rab3a recycling machinery and presynaptic activity

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; DISSOCIATION; MACHINERY; RECYCLING;

EID: 84875151201     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.AAC120.015921     Document Type: Erratum
Times cited : (85)

References (63)
  • 1
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • Cookson, M. R. (2005) The biochemistry of Parkinson's disease. Annu. Rev. Biochem. 74, 29-52
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 4
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of α-Synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani, V. M., Lu, W., Berge, V., Nakamura, K., Onoa, B., Lee, M. K., Chaudhry, F. A., Nicoll, R. A., and Edwards, R. H. (2010) Increased expression of α-Synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 65, 66-79
    • (2010) Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5    Lee, M.K.6    Chaudhry, F.A.7    Nicoll, R.A.8    Edwards, R.H.9
  • 5
    • 77953796839 scopus 로고    scopus 로고
    • A pathologic cascade leading to synaptic dysfunction in α-Synuclein-induced neurodegeneration
    • Scott, D. A., Tabarean, I., Tang, Y., Cartier, A., Masliah, E., and Roy, S. (2010) A pathologic cascade leading to synaptic dysfunction in α-Synuclein-induced neurodegeneration. J. Neurosci. 30, 8083-8095
    • (2010) J. Neurosci. , vol.30 , pp. 8083-8095
    • Scott, D.A.1    Tabarean, I.2    Tang, Y.3    Cartier, A.4    Masliah, E.5    Roy, S.6
  • 6
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and α-Synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy, D. D., Rueter, S. M., Trojanowski, J. Q., and Lee, V. M. (2000) Synucleins are developmentally expressed, and α-Synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J. Neurosci. 20, 3214-3220
    • (2000) J. Neurosci. , vol.20 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 7
    • 0029820770 scopus 로고    scopus 로고
    • Characterization of the precursor protein of the non-Aβ component of senile plaques (NACP) in the human central nervous system
    • Irizarry, M. C., Kim, T. W., McNamara, M., Tanzi, R. E., George, J. M., Clayton, D. F., and Hyman, B. T. (1996) Characterization of the precursor protein of the non-Aβ component of senile plaques (NACP) in the human central nervous system. J. Neuropathol. Exp. Neurol. 55, 889-895
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 889-895
    • Irizarry, M.C.1    Kim, T.W.2    McNamara, M.3    Tanzi, R.E.4    George, J.M.5    Clayton, D.F.6    Hyman, B.T.7
  • 11
    • 77952900626 scopus 로고    scopus 로고
    • α-Synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi, N., Helm, J. R., Nycz, D. C., Bentley, M., Liang, Y., and Hay, J. C. (2010) α-Synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs. Mol. Biol. Cell 21, 1850-1863
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 12
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., and Lansbury, P. T., Jr. (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35, 13709-13715
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr., P.T.5
  • 13
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-Synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W. S., Jonas, A., Clayton, D. F., and George, J. M. (1998) Stabilization of α-Synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273, 9443-9449
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 14
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-Synuclein in its free and lipid-associated states
    • Eliezer, D., Kutluay, E., Bussell, R., Jr., and Browne, G. (2001) Conformational properties of α-Synuclein in its free and lipid-associated states. J. Mol. Biol. 307, 1061-1073
    • (2001) J. Mol. Biol. , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell Jr., R.3    Browne, G.4
  • 15
    • 2942555022 scopus 로고    scopus 로고
    • Structure of membrane-boundα-Synuclein studied by site-directed spin labeling
    • Jao, C. C., Der-Sarkissian, A., Chen, J., and Langen, R. (2004) Structure of membrane-boundα-Synuclein studied by site-directed spin labeling. Proc. Natl. Acad. Sci. U.S.A. 101, 8331-8336
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 8331-8336
    • Jao, C.C.1    Der-Sarkissian, A.2    Chen, J.3    Langen, R.4
  • 17
    • 0026067472 scopus 로고
    • A small GTPbinding protein dissociates from synaptic vesicles during exocytosis
    • Fischer von Mollard, G., Südhof, T. C., and Jahn, R. (1991) A small GTPbinding protein dissociates from synaptic vesicles during exocytosis. Nature 349, 79-81
    • (1991) Nature , vol.349 , pp. 79-81
    • Fischer Von Mollard, G.1    Südhof, T.C.2    Jahn, R.3
  • 18
    • 0032125862 scopus 로고    scopus 로고
    • Differential regulation of exocytosis by calcium and CAPS in semi-intact synaptosomes
    • Tandon, A., Bannykh, S., Kowalchyk, J. A., Banerjee, A., Martin, T. F., and Balch, W. E. (1998) Differential regulation of exocytosis by calcium and CAPS in semi-intact synaptosomes. Neuron 21, 147-154
    • (1998) Neuron , vol.21 , pp. 147-154
    • Tandon, A.1    Bannykh, S.2    Kowalchyk, J.A.3    Banerjee, A.4    Martin, T.F.5    Balch, W.E.6
  • 20
    • 0037110754 scopus 로고    scopus 로고
    • Rab-αGDI activity is regulated by a Hsp90 chaperone complex
    • Sakisaka, T., Meerlo, T., Matteson, J., Plutner, H., and Balch, W. E. (2002) Rab-αGDI activity is regulated by a Hsp90 chaperone complex. EMBO J. 21, 6125-6135
    • (2002) EMBO J , vol.21 , pp. 6125-6135
    • Sakisaka, T.1    Meerlo, T.2    Matteson, J.3    Plutner, H.4    Balch, W.E.5
  • 21
    • 32344444043 scopus 로고    scopus 로고
    • Use of Hsp90 inhibitors to disrupt GDI-dependent Rab recycling
    • Chen, C. Y., Sakisaka, T., and Balch, W. E. (2005) Use of Hsp90 inhibitors to disrupt GDI-dependent Rab recycling. Methods Enzymol. 403, 339-347
    • (2005) Methods Enzymol , vol.403 , pp. 339-347
    • Chen, C.Y.1    Sakisaka, T.2    Balch, W.E.3
  • 23
    • 0026463861 scopus 로고
    • Amino acid residues in the Ras-like GTPase Rab3A that specify sensitivity to factors that regulate the GTP/GDP cycling of Rab3A
    • Burstein, E. S., Brondyk, W. H., and Macara, I. G. (1992) Amino acid residues in the Ras-like GTPase Rab3A that specify sensitivity to factors that regulate the GTP/GDP cycling of Rab3A. J. Biol. Chem. 267, 22715-22718
    • (1992) J. Biol. Chem. , vol.267 , pp. 22715-22718
    • Burstein, E.S.1    Brondyk, W.H.2    MacAra, I.G.3
  • 24
    • 0027158878 scopus 로고
    • Mutants of Rab3A analogous to oncogenic Ras mutants. Sensitivity to Rab3A-GTPase-activating protein and Rab3A-guanine nucleotide releasing factor
    • Brondyk, W. H., McKiernan, C. J., Burstein, E. S., and Macara, I. G. (1993) Mutants of Rab3A analogous to oncogenic Ras mutants. Sensitivity to Rab3A-GTPase-activating protein and Rab3A-guanine nucleotide releasing factor. J. Biol. Chem. 268, 9410-9415
    • (1993) J. Biol. Chem. , vol.268 , pp. 9410-9415
    • Brondyk, W.H.1    McKiernan, C.J.2    Burstein, E.S.3    MacAra, I.G.4
  • 25
    • 0037175049 scopus 로고    scopus 로고
    • Localization versus function of Rab3 proteins. Evidence for a common regulatory role in controlling fusion
    • Schlüter, O. M., Khvotchev, M., Jahn, R., and Südhof, T. C. (2002) Localization versus function of Rab3 proteins. Evidence for a common regulatory role in controlling fusion. J. Biol. Chem. 277, 40919-40929
    • (2002) J. Biol. Chem. , vol.277 , pp. 40919-40929
    • Schlüter, O.M.1    Khvotchev, M.2    Jahn, R.3    Südhof, T.C.4
  • 27
    • 39349092547 scopus 로고    scopus 로고
    • Core proteins of the secretory machinery
    • Lang, T., and Jahn, R. (2008) Core proteins of the secretory machinery. Handb. Exp. Pharmacol. 184, 107-127
    • (2008) Handb. Exp. Pharmacol. , vol.184 , pp. 107-127
    • Lang, T.1    Jahn, R.2
  • 29
    • 0034157347 scopus 로고    scopus 로고
    • A new functional domain of guanine nucleotide dissociation inhibitor (α-GDI) involved in Rab recycling
    • Luan, P., Heine, A., Zeng, K., Moyer, B., Greasely, S. E., Kuhn, P., Balch, W. E., and Wilson, I. A. (2000) A new functional domain of guanine nucleotide dissociation inhibitor (α-GDI) involved in Rab recycling. Traffic 1, 270-281
    • (2000) Traffic , vol.1 , pp. 270-281
    • Luan, P.1    Heine, A.2    Zeng, K.3    Moyer, B.4    Greasely, S.E.5    Kuhn, P.6    Balch, W.E.7    Wilson, I.A.8
  • 30
    • 3242879787 scopus 로고    scopus 로고
    • α-Synuclein-synaptosomal membrane interactions: Implications for fibrillogenesis
    • Jo, E., Darabie, A. A., Han, K., Tandon, A., Fraser, P. E., and McLaurin, J. (2004) α-Synuclein-synaptosomal membrane interactions: implications for fibrillogenesis. Eur. J. Biochem. 271, 3180-3189
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3180-3189
    • Jo, E.1    Darabie, A.A.2    Han, K.3    Tandon, A.4    Fraser, P.E.5    McLaurin, J.6
  • 32
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human α-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis
    • Perrin, R. J., Woods, W. S., Clayton, D. F., and George, J. M. (2000) Interaction of human α-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J. Biol. Chem. 275, 34393-34398
    • (2000) J. Biol. Chem. , vol.275 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 33
    • 0035928748 scopus 로고    scopus 로고
    • Membrane binding and self-association of α-Synucleins
    • Narayanan, V., and Scarlata, S. (2001) Membrane binding and self-association of α-Synucleins. Biochemistry 40, 9927-9934
    • (2001) Biochemistry , vol.40 , pp. 9927-9934
    • Narayanan, V.1    Scarlata, S.2
  • 34
    • 0141891097 scopus 로고    scopus 로고
    • The association of α-Synuclein with membranes affects bilayer structure, stability, and fibril formation
    • Zhu, M., Li, J., and Fink, A. L. (2003) The association of α-Synuclein with membranes affects bilayer structure, stability, and fibril formation. J. Biol. Chem. 278, 40186-40197
    • (2003) J. Biol. Chem. , vol.278 , pp. 40186-40197
    • Zhu, M.1    Li, J.2    Fink, A.L.3
  • 35
  • 36
    • 0036307753 scopus 로고    scopus 로고
    • Defective membrane interactions of familial Parkinson's disease mutant A30P α-Synuclein
    • Jo, E., Fuller, N., Rand, R. P., St George-Hyslop, P., and Fraser, P. E. (2002) Defective membrane interactions of familial Parkinson's disease mutant A30P α-Synuclein. J. Mol. Biol. 315, 799-807
    • (2002) J. Mol. Biol. , vol.315 , pp. 799-807
    • Jo, E.1    Fuller, N.2    Rand, R.P.3    St George-Hyslop, P.4    Fraser, P.E.5
  • 37
    • 0032500599 scopus 로고    scopus 로고
    • Binding of α-Synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • Jensen, P. H., Nielsen, M. S., Jakes, R., Dotti, C. G., and Goedert, M. (1998) Binding of α-Synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J. Biol. Chem. 273, 26292-26294
    • (1998) J. Biol. Chem. , vol.273 , pp. 26292-26294
    • Jensen, P.H.1    Nielsen, M.S.2    Jakes, R.3    Dotti, C.G.4    Goedert, M.5
  • 38
    • 1942534598 scopus 로고    scopus 로고
    • Effects of Parkinson's disease-linked mutations on the structure of lipid-associated α-Synuclein
    • Bussell, R., Jr., and Eliezer, D. (2004) Effects of Parkinson's disease-linked mutations on the structure of lipid-associated α-Synuclein. Biochemistry 43, 4810-4818
    • (2004) Biochemistry , vol.43 , pp. 4810-4818
    • Bussell Jr., R.1    Eliezer, D.2
  • 40
    • 18044381951 scopus 로고    scopus 로고
    • α-Synuclein binding to rab3a in multiple system atrophy
    • Dalfó, E., and Ferrer, I. (2005) α-Synuclein binding to rab3a in multiple system atrophy. Neurosci. Lett. 380, 170-175
    • (2005) Neurosci. Lett. , vol.380 , pp. 170-175
    • Dalfó, E.1    Ferrer, I.2
  • 41
    • 2342457804 scopus 로고    scopus 로고
    • Abnormal α-Synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease
    • Dalfó, E., Barrachina, M., Rosa, J. L., Ambrosio, S., and Ferrer, I. (2004) Abnormal α-Synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease. Neurobiol. Dis. 16, 92-97
    • (2004) Neurobiol. Dis. , vol.16 , pp. 92-97
    • Dalfó, E.1    Barrachina, M.2    Rosa, J.L.3    Ambrosio, S.4    Ferrer, I.5
  • 46
    • 52549126992 scopus 로고    scopus 로고
    • Regulation of secretory vesicle traffic by Rab small GTPases
    • Fukuda, M. (2008) Regulation of secretory vesicle traffic by Rab small GTPases. Cell. Mol. Life Sci. 65, 2801-2813
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2801-2813
    • Fukuda, M.1
  • 47
    • 23844445866 scopus 로고    scopus 로고
    • The structural and mechanistic basis for recycling of Rab proteins between membrane compartments
    • Goody, R. S., Rak, A., and Alexandrov, K. (2005) The structural and mechanistic basis for recycling of Rab proteins between membrane compartments. Cell. Mol. Life Sci. 62, 1657-1670
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1657-1670
    • Goody, R.S.1    Rak, A.2    Alexandrov, K.3
  • 49
    • 0025830577 scopus 로고
    • C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester
    • Farnsworth, C. C., Kawata, M., Yoshida, Y., Takai, Y., Gelb, M. H., and Glomset, J. A. (1991) C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester. Proc. Natl. Acad. Sci. U.S.A. 88, 6196-6200
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 6196-6200
    • Farnsworth, C.C.1    Kawata, M.2    Yoshida, Y.3    Takai, Y.4    Gelb, M.H.5    Glomset, J.A.6
  • 50
    • 0026668873 scopus 로고
    • The geranylgeranyl moiety but not the methyl moiety of the smg-25A/rab3A protein is essential for the interactions with membrane and its inhibitory GDP/GTP exchange protein
    • Musha, T., Kawata, M., and Takai, Y. (1992) The geranylgeranyl moiety but not the methyl moiety of the smg-25A/rab3A protein is essential for the interactions with membrane and its inhibitory GDP/GTP exchange protein. J. Biol. Chem. 267, 9821-9825
    • (1992) J. Biol. Chem. , vol.267 , pp. 9821-9825
    • Musha, T.1    Kawata, M.2    Takai, Y.3
  • 52
    • 0033591317 scopus 로고    scopus 로고
    • Molecular dissection of guanine nucleotide dissociation inhibitor function in vivo. Rabindependent binding to membranes and role of Rab recycling factors
    • Luan, P., Balch, W. E., Emr, S. D., and Burd, C. G. (1999) Molecular dissection of guanine nucleotide dissociation inhibitor function in vivo. Rabindependent binding to membranes and role of Rab recycling factors. J. Biol. Chem. 274, 14806-14817
    • (1999) J. Biol. Chem. , vol.274 , pp. 14806-14817
    • Luan, P.1    Balch, W.E.2    Emr, S.D.3    Burd, C.G.4
  • 56
    • 84857059950 scopus 로고    scopus 로고
    • CSPα knockout causes neurodegeneration by impairing SNAP-25 function
    • Sharma, M., Burré, J., Bronk, P., Zhang, Y., Xu, W., and Südhof, T. C. (2012) CSPα knockout causes neurodegeneration by impairing SNAP-25 function. EMBO J. 31, 829-841
    • (2012) EMBO J , vol.31 , pp. 829-841
    • Sharma, M.1    Burré, J.2    Bronk, P.3    Zhang, Y.4    Xu, W.5    Südhof, T.C.6
  • 57
    • 78650505099 scopus 로고    scopus 로고
    • CSPα promotes SNARE complex assembly by chaperoning SNAP-25 during synaptic activity
    • Sharma, M., Burré, J., and Südhof, T. C. (2011) CSPα promotes SNARE complex assembly by chaperoning SNAP-25 during synaptic activity. Nat. Cell Biol. 13, 30-39
    • (2011) Nat. Cell Biol. , vol.13 , pp. 30-39
    • Sharma, M.1    Burré, J.2    Südhof, T.C.3
  • 58
  • 60
    • 0036786216 scopus 로고    scopus 로고
    • Evidence that α-Synuclein functions as a negative regulator of Ca2+-dependent α-granule release from human platelets
    • Park, S. M., Jung, H. Y., Kim, H. O., Rhim, H., Paik, S. R., Chung, K. C., Park, J. H., and Kim, J. (2002) Evidence that α-Synuclein functions as a negative regulator of Ca2+-dependent α-granule release from human platelets. Blood 100, 2506-2514
    • (2002) Blood , vol.100 , pp. 2506-2514
    • Park, S.M.1    Jung, H.Y.2    Kim, H.O.3    Rhim, H.4    Paik, S.R.5    Chung, K.C.6    Park, J.H.7    Kim, J.8
  • 62
    • 77954368879 scopus 로고    scopus 로고
    • Regulation of Weibel-Palade body exocytosis by α-Synuclein in endothelial cells
    • Kim, K. S., Park, J. Y., Jou, I., and Park, S. M. (2010) Regulation of Weibel-Palade body exocytosis by α-Synuclein in endothelial cells. J. Biol. Chem. 285, 21416-21425
    • (2010) J. Biol. Chem. , vol.285 , pp. 21416-21425
    • Kim, K.S.1    Park, J.Y.2    Jou, I.3    Park, S.M.4
  • 63
    • 84864258151 scopus 로고    scopus 로고
    • α-Synuclein inhibits intersynaptic vesicle mobility and maintains recycling-pool homeostasis
    • Scott, D., and Roy, S. (2012) α-Synuclein inhibits intersynaptic vesicle mobility and maintains recycling-pool homeostasis. J. Neurosci. 32, 10129-10135
    • (2012) J. Neurosci. , vol.32 , pp. 10129-10135
    • Scott, D.1    Roy, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.