메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

A genome-wide imaging-based screening to identify genes involved in synphilin-1 inclusion formation in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN;

EID: 84979500315     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep30134     Document Type: Article
Times cited : (10)

References (45)
  • 1
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • Baba, M. et al. Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. The American journal of pathology 152, 879-884 (1998).
    • (1998) The American Journal of Pathology , vol.152 , pp. 879-884
    • Baba, M.1
  • 2
    • 0034085796 scopus 로고    scopus 로고
    • Synphilin-1 is present in Lewy bodies in Parkinson's disease
    • Wakabayashi, K. et al. Synphilin-1 is present in Lewy bodies in Parkinson's disease. Ann Neurol 47, 521-523, doi: 10.1002/1531-8249(200004)47:4<521::Aid-Ana18>3.0.Co;2-B (2000).
    • (2000) Ann Neurol , vol.47 , pp. 521-523
    • Wakabayashi, K.1
  • 3
    • 0032952414 scopus 로고    scopus 로고
    • Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions
    • Engelender, S. et al. Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions. Nature genetics 22, 110-114, doi: 10.1038/8820 (1999).
    • (1999) Nature Genetics , vol.22 , pp. 110-114
    • Engelender, S.1
  • 4
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body formation in Parkinson disease
    • Chung, K. K. et al. Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nature medicine 7, 1144-1150, doi: 10.1038/nm1001-1144 (2001).
    • (2001) Nature Medicine , vol.7 , pp. 1144-1150
    • Chung, K.K.1
  • 5
    • 0042206574 scopus 로고    scopus 로고
    • Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1
    • Ito, T. et al. Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1. The Journal of biological chemistry 278, 29106-29114, doi: 10.1074/jbc.M302763200 (2003).
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 29106-29114
    • Ito, T.1
  • 6
    • 0037189591 scopus 로고    scopus 로고
    • Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein
    • Ribeiro, C. S., Carneiro, K., Ross, C. A., Menezes, J. R. L. & Engelender, S. Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein. Journal of Biological Chemistry 277, 23927-23933, doi: 10.1074/jbc.M201115200 (2002).
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 23927-23933
    • Ribeiro, C.S.1    Carneiro, K.2    Ross, C.A.3    Menezes, J.R.L.4    Engelender, S.5
  • 7
    • 78149449581 scopus 로고    scopus 로고
    • Synphilin-1 enhances alpha-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent manner
    • Buttner, S. et al. Synphilin-1 enhances alpha-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent manner. PloS one 5, e13700, doi: 10.1371/journal.pone.0013700 (2010).
    • (2010) PloS One , vol.5 , pp. e13700
    • Buttner, S.1
  • 8
    • 75649111192 scopus 로고    scopus 로고
    • The genetic landscape of a cell
    • Costanzo, M. et al. The genetic landscape of a cell. Science 327, 425-431, doi: 10.1126/science.1180823 (2010).
    • (2010) Science , vol.327 , pp. 425-431
    • Costanzo, M.1
  • 9
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • Tong, A. H. Y. et al. Systematic Genetic Analysis with Ordered Arrays of Yeast Deletion Mutants. Science 294, 2364-2368, doi: 10.1126/science.1065810 (2001).
    • (2001) Science , vol.294 , pp. 2364-2368
    • Tong, A.H.Y.1
  • 10
    • 10744230485 scopus 로고    scopus 로고
    • Global mapping of the yeast genetic interaction network
    • Tong, A. H. Y. et al. Global Mapping of the Yeast Genetic Interaction Network. Science 303, 808-813, doi: 10.1126/science.1091317 (2004).
    • (2004) Science , vol.303 , pp. 808-813
    • Tong, A.H.Y.1
  • 11
    • 75749095658 scopus 로고    scopus 로고
    • Integrating high-throughput genetic interaction mapping and high-content screening to explore yeast spindle morphogenesis
    • Vizeacoumar, F. J. et al. Integrating high-throughput genetic interaction mapping and high-content screening to explore yeast spindle morphogenesis. The Journal of cell biology 188, 69-81, doi: 10.1083/jcb.200909013 (2010).
    • (2010) The Journal of Cell Biology , vol.188 , pp. 69-81
    • Vizeacoumar, F.J.1
  • 12
    • 84930684870 scopus 로고    scopus 로고
    • Yeast proteome dynamics from single cell imaging and automated analysis
    • Chong, Y. T. et al. Yeast Proteome Dynamics from Single Cell Imaging and Automated Analysis. Cell 161, 1413-1424, doi: 10.1016/j. cell.2015.04.051 (2015).
    • (2015) Cell , vol.161 , pp. 1413-1424
    • Chong, Y.T.1
  • 13
    • 84912083665 scopus 로고    scopus 로고
    • Stress granule-defective mutants deregulate stress responsive transcripts
    • Yang, X. X. et al. Stress Granule-Defective Mutants Deregulate Stress Responsive Transcripts. Plos Genet 10, doi: 10.1371/journal. pgen.1004763 (2014).
    • (2014) Plos Genet , pp. 10
    • Yang, X.X.1
  • 14
    • 84930577438 scopus 로고    scopus 로고
    • Lipid droplets are essential for efficient clearance of cytosolic inclusion bodies
    • Moldavski, O. et al. Lipid Droplets Are Essential for Efficient Clearance of Cytosolic Inclusion Bodies. Developmental cell 33, 603-610, doi: 10.1016/j.devcel.2015.04.015 (2015).
    • (2015) Developmental Cell , vol.33 , pp. 603-610
    • Moldavski, O.1
  • 15
    • 80053372157 scopus 로고    scopus 로고
    • Aggresome formation and segregation of inclusions influence toxicity of alpha-synuclein and synphilin-1 in yeast
    • Swinnen, E. et al. Aggresome formation and segregation of inclusions influence toxicity of alpha-synuclein and synphilin-1 in yeast. Biochemical Society transactions 39, 1476-1481, doi: 10.1042/BST0391476 (2011).
    • (2011) Biochemical Society Transactions , vol.39 , pp. 1476-1481
    • Swinnen, E.1
  • 16
    • 84862262073 scopus 로고    scopus 로고
    • YeastMine-an integrated data warehouse for Saccharomyces cerevisiae data as a multipurpose tool-kit
    • Balakrishnan, R. et al. YeastMine-an integrated data warehouse for Saccharomyces cerevisiae data as a multipurpose tool-kit. Database : the journal of biological databases and curation 2012, bar062, doi: 10.1093/database/bar062 (2012).
    • (2012) Database : The Journal of Biological Databases and Curation , vol.2012 , pp. bar062
    • Balakrishnan, R.1
  • 17
    • 84905484568 scopus 로고    scopus 로고
    • Essential genetic interactors of SIR2 required for spatial sequestration and asymmetrical inheritance of protein aggregates
    • Song, J. et al. Essential genetic interactors of SIR2 required for spatial sequestration and asymmetrical inheritance of protein aggregates. PLoS genetics 10, e1004539, doi: 10.1371/journal.pgen.1004539 (2014).
    • (2014) PLoS Genetics , vol.10 , pp. e1004539
    • Song, J.1
  • 18
    • 81855218130 scopus 로고    scopus 로고
    • Segregation of protein aggregates involves actin and the polarity machinery
    • Liu, B. et al. Segregation of protein aggregates involves actin and the polarity machinery. Cell 147, 959-961, doi: 10.1016/j. cell.2011.11.018 (2011).
    • (2011) Cell , vol.147 , pp. 959-961
    • Liu, B.1
  • 19
    • 74549184412 scopus 로고    scopus 로고
    • The polarisome is required for segregation and retrograde transport of protein aggregates
    • Liu, B. et al. The polarisome is required for segregation and retrograde transport of protein aggregates. Cell 140, 257-267, doi: 10.1016/j.cell.2009.12.031 (2010).
    • (2010) Cell , vol.140 , pp. 257-267
    • Liu, B.1
  • 20
    • 67749142344 scopus 로고    scopus 로고
    • Function of dynein in budding yeast: Mitotic spindle positioning in a polarized cell
    • Moore, J. K., Stuchell-Brereton, M. D. & Cooper, J. A. Function of dynein in budding yeast: mitotic spindle positioning in a polarized cell. Cell Motil Cytoskeleton 66, 546-555, doi: 10.1002/cm.20364 (2009).
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 546-555
    • Moore, J.K.1    Stuchell-Brereton, M.D.2    Cooper, J.A.3
  • 22
    • 40449130757 scopus 로고    scopus 로고
    • Dynactin function in mitotic spindle positioning
    • Moore, J. K., Li, J. & Cooper, J. A. Dynactin function in mitotic spindle positioning. Traffic 9, 510-527, doi: 10.1111/j.1600-0854.2008.00710.x (2008).
    • (2008) Traffic , vol.9 , pp. 510-527
    • Moore, J.K.1    Li, J.2    Cooper, J.A.3
  • 23
    • 1042266326 scopus 로고    scopus 로고
    • Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
    • Tanaka, M. et al. Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. The Journal of biological chemistry 279, 4625-4631, doi: 10.1074/jbc.M310994200 (2004).
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 4625-4631
    • Tanaka, M.1
  • 24
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R. Aggresomes, inclusion bodies and protein aggregation. Trends in cell biology 10, 524-530 (2000).
    • (2000) Trends in Cell Biology , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 25
    • 55549105778 scopus 로고    scopus 로고
    • Triggering aggresome formation. Dissecting aggresome-targeting and aggregation signals in synphilin 1
    • Zaarur, N., Meriin, A. B., Gabai, V. L. & Sherman, M. Y. Triggering aggresome formation. Dissecting aggresome-targeting and aggregation signals in synphilin 1. The Journal of biological chemistry 283, 27575-27584, doi: 10.1074/jbc.M802216200 (2008).
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 27575-27584
    • Zaarur, N.1    Meriin, A.B.2    Gabai, V.L.3    Sherman, M.Y.4
  • 26
    • 0032577573 scopus 로고    scopus 로고
    • Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
    • Vainberg, I. E. et al. Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93, 863-873 (1998).
    • (1998) Cell , vol.93 , pp. 863-873
    • Vainberg, I.E.1
  • 27
    • 0034611628 scopus 로고    scopus 로고
    • Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT
    • Leroux, M. R. & Hartl, F. U. Protein folding: versatility of the cytosolic chaperonin TRiC/CCT. Current biology : CB. 10, R260-R264 (2000).
    • (2000) Current Biology : CB , vol.10 , pp. R260-R264
    • Leroux, M.R.1    Hartl, F.U.2
  • 28
    • 30644474711 scopus 로고    scopus 로고
    • Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast
    • Ganusova, E. E. et al. Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Molecular and cellular biology 26, 617-629, doi: 10.1128/MCB.26.2.617-629.2006 (2006).
    • (2006) Molecular and Cellular Biology , vol.26 , pp. 617-629
    • Ganusova, E.E.1
  • 29
    • 79960467038 scopus 로고    scopus 로고
    • Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton
    • Chernova, T. A. et al. Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Molecular cell 43, 242-252, doi: 10.1016/j.molcel.2011.07.001 (2011).
    • (2011) Molecular Cell , vol.43 , pp. 242-252
    • Chernova, T.A.1
  • 30
    • 0032832981 scopus 로고    scopus 로고
    • Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae
    • Bailleul, P. A., Newnam, G. P., Steenbergen, J. N. & Chernoff, Y. O. Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Genetics 153, 81-94 (1999).
    • (1999) Genetics , vol.153 , pp. 81-94
    • Bailleul, P.A.1    Newnam, G.P.2    Steenbergen, J.N.3    Chernoff, Y.O.4
  • 31
    • 0035947084 scopus 로고    scopus 로고
    • Identification of RFC(Ctf18p, Ctf8p, Dcc1p): An alternative RFC complex required for sister chromatid cohesion in S. Cerevisiae
    • Mayer, M. L., Gygi, S. P., Aebersold, R. & Hieter, P. Identification of RFC(Ctf18p, Ctf8p, Dcc1p): an alternative RFC complex required for sister chromatid cohesion in S. cerevisiae. Molecular cell 7, 959-970 (2001).
    • (2001) Molecular Cell , vol.7 , pp. 959-970
    • Mayer, M.L.1    Gygi, S.P.2    Aebersold, R.3    Hieter, P.4
  • 32
    • 33748424969 scopus 로고    scopus 로고
    • Establishment of sister chromatid cohesion at the S. Cerevisiae replication fork
    • Lengronne, A. et al. Establishment of sister chromatid cohesion at the S. cerevisiae replication fork. Molecular cell 23, 787-799, doi: 10.1016/j.molcel.2006.08.018 (2006).
    • (2006) Molecular Cell , vol.23 , pp. 787-799
    • Lengronne, A.1
  • 33
    • 77954128788 scopus 로고    scopus 로고
    • Hyperphosphatasia with seizures, neurologic deficit, and characteristic facial features: Five new patients with Mabry syndrome
    • Thompson, M. D. et al. Hyperphosphatasia with seizures, neurologic deficit, and characteristic facial features: Five new patients with Mabry syndrome. American journal of medical genetics. Part A. 152A, 1661-1669, doi: 10.1002/ajmg.a.33438 (2010).
    • (2010) American Journal of Medical Genetics. Part A , vol.152 A , pp. 1661-1669
    • Thompson, M.D.1
  • 34
    • 20344394154 scopus 로고    scopus 로고
    • Anchorless prion protein results in infectious amyloid disease without clinical scrapie
    • Chesebro, B. et al. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. science 308, 1435-1439, doi: 10.1126/science.1110837 (2005).
    • (2005) Science , vol.308 , pp. 1435-1439
    • Chesebro, B.1
  • 35
    • 33746362894 scopus 로고    scopus 로고
    • Interactions of Synphilin-1 with phospholipids and lipid membranes
    • Takahashi, T. et al. Interactions of Synphilin-1 with phospholipids and lipid membranes. FEBS Lett. 580, 4479-4484, doi: 10.1016/j. febslet.2006.07.019 (2006).
    • (2006) FEBS Lett. , vol.580 , pp. 4479-4484
    • Takahashi, T.1
  • 36
    • 0033562333 scopus 로고    scopus 로고
    • A role for Ctr9p and Paf1p in the regulation G1 cyclin expression in yeast
    • Koch, C., Wollmann, P., Dahl, M. & Lottspeich, F. A role for Ctr9p and Paf1p in the regulation G1 cyclin expression in yeast. Nucleic Acids Res. 27, 2126-2134 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2126-2134
    • Koch, C.1    Wollmann, P.2    Dahl, M.3    Lottspeich, F.4
  • 37
    • 0037524702 scopus 로고    scopus 로고
    • The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: Linking transcriptional elongation to histone methylation
    • Krogan, N. J. et al. The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11, 721-729 (2003).
    • (2003) Mol Cell , vol.11 , pp. 721-729
    • Krogan, N.J.1
  • 38
    • 67649374865 scopus 로고    scopus 로고
    • Protein misfolding and aggregation in Parkinson's disease
    • Tan, J. M., Wong, E. S. & Lim, K. L. Protein misfolding and aggregation in Parkinson's disease. Antioxidants & redox signaling 11, 2119-2134, doi: 10.1089/ARS.2009.2490 (2009).
    • (2009) Antioxidants & Redox Signaling , vol.11 , pp. 2119-2134
    • Tan, J.M.1    Wong, E.S.2    Lim, K.L.3
  • 39
    • 80052290024 scopus 로고    scopus 로고
    • Glutamate dehydrogenase in brain mitochondria: Do lipid modifications and transient metabolon formation influence enzyme activity?
    • McKenna, M. C. Glutamate dehydrogenase in brain mitochondria: do lipid modifications and transient metabolon formation influence enzyme activity? Neurochemistry international 59, 525-533, doi: 10.1016/j.neuint.2011.07.003 (2011).
    • (2011) Neurochemistry International , vol.59 , pp. 525-533
    • McKenna, M.C.1
  • 40
    • 0034085796 scopus 로고    scopus 로고
    • Synphilin-1 is present in Lewy bodies in Parkinson's disease
    • Wakabayashi, K. et al. Synphilin-1 is present in Lewy bodies in Parkinson's disease. Annals of neurology 47, 521-523 (2000).
    • (2000) Annals of Neurology , vol.47 , pp. 521-523
    • Wakabayashi, K.1
  • 41
    • 79953845487 scopus 로고    scopus 로고
    • Systematic exploration of essential yeast gene function with temperature-sensitive mutants
    • Li, Z. et al. Systematic exploration of essential yeast gene function with temperature-sensitive mutants. Nature biotechnology 29, 361-367, doi: 10.1038/nbt.1832 (2011).
    • (2011) Nature Biotechnology , vol.29 , pp. 361-367
    • Li, Z.1
  • 42
    • 64349112353 scopus 로고    scopus 로고
    • A molecular barcoded yeast ORF library enables mode-of-action analysis of bioactive compounds
    • Ho, C. H. et al. A molecular barcoded yeast ORF library enables mode-of-action analysis of bioactive compounds. Nature biotechnology 27, 369-377, doi: 10.1038/nbt.1534 (2009).
    • (2009) Nature Biotechnology , vol.27 , pp. 369-377
    • Ho, C.H.1
  • 43
    • 12344269924 scopus 로고    scopus 로고
    • GO: TermFinder-open source software for accessing Gene Ontology information and finding significantly enriched Gene Ontology terms associated with a list of genes
    • Boyle, E. I. et al. GO: TermFinder-open source software for accessing Gene Ontology information and finding significantly enriched Gene Ontology terms associated with a list of genes. Bioinformatics 20, 3710-3715, doi: 10.1093/bioinformatics/bth456 (2004).
    • (2004) Bioinformatics , vol.20 , pp. 3710-3715
    • Boyle, E.I.1
  • 45
    • 38549173606 scopus 로고    scopus 로고
    • The BioGRID interaction database: 2008 update
    • Breitkreutz, B. J. et al. The BioGRID Interaction Database: 2008 update. Nucleic Acids Res. 36, D637-640 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. D637-640
    • Breitkreutz, B.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.