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Volumn 7, Issue 1, 2017, Pages

A cluster of palmitoylated cysteines are essential for aggregation of cysteine-string protein mutants that cause neuronal ceroid lipofuscinosis

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; CYSTEINE STRING PROTEIN; HEAT SHOCK PROTEIN 40; MEMBRANE PROTEIN;

EID: 85017963868     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-017-00036-8     Document Type: Article
Times cited : (27)

References (19)
  • 1
    • 84995581912 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative diseases: From theory to therapy
    • Kumar, V. et al. Protein aggregation and neurodegenerative diseases: From theory to therapy. Eur. J. Med. Chem. 124, 1105-1120 (2016).
    • (2016) Eur. J. Med. Chem. , vol.124 , pp. 1105-1120
    • Kumar, V.1
  • 2
    • 84937804600 scopus 로고    scopus 로고
    • Protein aggregation and neurodegeneration in prototypical neurodegenerative diseases: Examples of amyloidopathies, tauopathies and synucleinopathies
    • Bourdenx, M. et al. Protein aggregation and neurodegeneration in prototypical neurodegenerative diseases: Examples of amyloidopathies, tauopathies and synucleinopathies. Prog. Neurobiol. doi:10.1016/j.pneurobio.2015.07.003 (2015).
    • (2015) Prog. Neurobiol.
    • Bourdenx, M.1
  • 4
    • 80051672679 scopus 로고    scopus 로고
    • Mutations in DNAJC5, Encoding Cysteine-String Protein Alpha, Cause Autosomal-Dominant Adult-Onset Neuronal Ceroid Lipofuscinosis
    • Noskova, L. et al. Mutations in DNAJC5, Encoding Cysteine-String Protein Alpha, Cause Autosomal-Dominant Adult-Onset Neuronal Ceroid Lipofuscinosis. Am. J. Human Genet 89, 241-252 (2011).
    • (2011) Am. J. Human Genet , vol.89 , pp. 241-252
    • Noskova, L.1
  • 5
    • 80455149806 scopus 로고    scopus 로고
    • Exome-Sequencing Confirms DNAJC5 Mutations as Cause of Adult Neuronal Ceroid-Lipofuscinosis
    • Benitez, B. A. et al. Exome-Sequencing Confirms DNAJC5 Mutations as Cause of Adult Neuronal Ceroid-Lipofuscinosis. PLoS ONE 6, e26741 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e26741
    • Benitez, B.A.1
  • 6
    • 84868261172 scopus 로고    scopus 로고
    • Palmitoylation-induced aggregation of cysteine-string protein mutants that cause neuronal ceroid lipofuscinosis
    • Greaves, J. et al. Palmitoylation-induced aggregation of cysteine-string protein mutants that cause neuronal ceroid lipofuscinosis. J. Biol. Chem 287, 37330-37339 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 37330-37339
    • Greaves, J.1
  • 7
  • 8
    • 0034051803 scopus 로고    scopus 로고
    • Cysteine-String Protein. The Chaperone at the Synapse
    • Chamberlain, L. H. & Burgoyne, R. D. Cysteine-String Protein. The Chaperone at the Synapse. J. Neurochem. 74, 1781-1789 (2000).
    • (2000) J. Neurochem. , vol.74 , pp. 1781-1789
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 9
    • 84920852152 scopus 로고    scopus 로고
    • Proteomics of protein post-translational modifications implicated in neurodegeneration
    • Ren, R. J., Dammer, E. B., Wang, G., Seyfried, N. T. & Levey, A. I. Proteomics of protein post-translational modifications implicated in neurodegeneration. Transl. Neurodegener 3, 23 (2014).
    • (2014) Transl. Neurodegener , vol.3 , pp. 23
    • Ren, R.J.1    Dammer, E.B.2    Wang, G.3    Seyfried, N.T.4    Levey, A.I.5
  • 10
    • 79952105548 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein: Implications for Alzheimer's disease
    • Martin, L., Latypova, X. & Terro, F. Post-translational modifications of tau protein: implications for Alzheimer's disease. Neurochem. Int. 58, 458-471 (2011).
    • (2011) Neurochem. Int. , vol.58 , pp. 458-471
    • Martin, L.1    Latypova, X.2    Terro, F.3
  • 11
    • 63149139630 scopus 로고    scopus 로고
    • Post-translational modifications of expanded polyglutamine proteins: Impact on neurotoxicity
    • Pennuto, M., Palazzolo, I. & Poletti, A. Post-translational modifications of expanded polyglutamine proteins: impact on neurotoxicity. Hum. Mol. Genet. 18, R40-47 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , pp. R40-R47
    • Pennuto, M.1    Palazzolo, I.2    Poletti, A.3
  • 12
    • 33745627659 scopus 로고    scopus 로고
    • Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function
    • Yanai, A. et al. Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function. Nat. Neurosci. 9, 824-831 (2006).
    • (2006) Nat. Neurosci. , vol.9 , pp. 824-831
    • Yanai, A.1
  • 13
    • 84908078138 scopus 로고    scopus 로고
    • Oligomerization of Cysteine String Protein alpha mutants causing adult neuronal ceroid lipofuscinosis
    • Zhang, Y.-q & Chandra, S. S. Oligomerization of Cysteine String Protein alpha mutants causing adult neuronal ceroid lipofuscinosis. Biochim. Biophys. Acta (BBA) - Molecular Basis of Disease 1842, 2136-2146 (2014).
    • (2014) Biochim. Biophys. Acta (BBA) - Molecular Basis of Disease , vol.1842 , pp. 2136-2146
    • Zhang, Y.-Q.1    Chandra, S.S.2
  • 15
    • 84961167751 scopus 로고    scopus 로고
    • Neuronal ceroid lipofuscinosis with DNAJC5/CSPalpha mutation has PPT1 pathology and exhibit aberrant protein palmitoylation
    • Henderson, M. X. et al. Neuronal ceroid lipofuscinosis with DNAJC5/CSPalpha mutation has PPT1 pathology and exhibit aberrant protein palmitoylation. Acta neuropathologica 131, 621-637 (2016).
    • (2016) Acta Neuropathologica , vol.131 , pp. 621-637
    • Henderson, M.X.1
  • 16
    • 0029153109 scopus 로고
    • Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis
    • Vesa, J. et al. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature 376, 584-587 (1995).
    • (1995) Nature , vol.376 , pp. 584-587
    • Vesa, J.1
  • 17
    • 33750516084 scopus 로고    scopus 로고
    • Dual Role of the Cysteine-String Domain in Membrane Binding and Palmitoylation-dependent Sorting of the Molecular Chaperone Cysteine-String Protein
    • Greaves, J. & Chamberlain, L. H. Dual Role of the Cysteine-String Domain in Membrane Binding and Palmitoylation-dependent Sorting of the Molecular Chaperone Cysteine-String Protein. Mol. Biol. Cell 17, 4748-4759 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4748-4759
    • Greaves, J.1    Chamberlain, L.H.2
  • 18
    • 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, L. H. Palmitoylation and Membrane Interactions of the Neuroprotective Chaperone Cysteine-string Protein. J. Biol. Chem. 283, 25014-25026 (2008).
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.