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Volumn 7, Issue 1, 2017, Pages

Deviation of the typical AAA substrate-threading pore prevents fatal protein degradation in yeast Cdc48

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AROMATIC AMINO ACID; CDC48 PROTEIN, S CEREVISIAE; PROTEASOME; SACCHAROMYCES CEREVISIAE PROTEIN; VALOSIN CONTAINING PROTEIN;

EID: 85024369024     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-017-05806-y     Document Type: Article
Times cited : (20)

References (48)
  • 1
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura, T. & Wilkinson, A. J. AAA+ superfamily ATPases: common structure-diverse function. Genes to Cells 6, 575-597 (2001).
    • (2001) Genes to Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 2
    • 39449115385 scopus 로고    scopus 로고
    • AAA+ proteins: Diversity in function, similarity in structure
    • Snider, J. & Houry, W. A. AAA+ proteins: diversity in function, similarity in structure. Biochem. Soc. Trans. 36, 72-77 (2008).
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 72-77
    • Snider, J.1    Houry, W.A.2
  • 5
    • 39449087857 scopus 로고    scopus 로고
    • From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins
    • Ogura, T. et al. From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins. Biochem. Soc. Trans. 36, 68-71 (2008).
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 68-71
    • Ogura, T.1
  • 6
    • 84855198122 scopus 로고    scopus 로고
    • Structure and function of the bacterial AAA protease FtsH
    • Langklotz, S., Baumann, U. & Narberhaus, F. Structure and function of the bacterial AAA protease FtsH. Biochim. Biophys. Acta 1823, 40-48 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 40-48
    • Langklotz, S.1    Baumann, U.2    Narberhaus, F.3
  • 7
    • 0348010363 scopus 로고    scopus 로고
    • Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis
    • Yamada-Inagawa, T., Okuno, T., Karata, K., Yamanaka, K. & Ogura, T. Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis. J. Biol. Chem. 278, 50182-50187 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 50182-50187
    • Yamada-Inagawa, T.1    Okuno, T.2    Karata, K.3    Yamanaka, K.4    Ogura, T.5
  • 8
    • 3042642040 scopus 로고    scopus 로고
    • Substrate recognition by the AAA+ chaperone ClpB
    • Schlieker, C. et al. Substrate recognition by the AAA+ chaperone ClpB. Nat. Struct. Mol. Biol. 11, 607-615 (2004).
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 607-615
    • Schlieker, C.1
  • 9
    • 84928822612 scopus 로고    scopus 로고
    • Microtubule severing by katanin p60 AAA+ ATPase requires the C-terminal acidic tails of both α- And β-tubulins and basic amino acid residues in the AAA+ ring pore
    • Johjima, A. et al. Microtubule severing by katanin p60 AAA+ ATPase requires the C-terminal acidic tails of both α- and β-tubulins and basic amino acid residues in the AAA+ ring pore. J. Biol. Chem. 290, 11762-11770 (2015).
    • (2015) J. Biol. Chem , vol.290 , pp. 11762-11770
    • Johjima, A.1
  • 10
    • 68049107472 scopus 로고    scopus 로고
    • Conserved aromatic and basic amino acid residues in the pore region of Caenorhabditis elegans spastin play critical roles in microtubule severing
    • Matsushita-Ishiodori, Y., Yamanaka, K., Hashimoto, H., Esaki, M. & Ogura, T. Conserved aromatic and basic amino acid residues in the pore region of Caenorhabditis elegans spastin play critical roles in microtubule severing. Genes to cells 14, 925-940 (2009).
    • (2009) Genes to Cells , vol.14 , pp. 925-940
    • Matsushita-Ishiodori, Y.1    Yamanaka, K.2    Hashimoto, H.3    Esaki, M.4    Ogura, T.5
  • 11
    • 84855206731 scopus 로고    scopus 로고
    • Recent advances in p97/VCP/Cdc48 cellular functions
    • Yamanaka, K., Sasagawa, Y. & Ogura, T. Recent advances in p97/VCP/Cdc48 cellular functions. Biochim. Biophys. Acta 1823, 130-137 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 130-137
    • Yamanaka, K.1    Sasagawa, Y.2    Ogura, T.3
  • 12
    • 84855195340 scopus 로고    scopus 로고
    • Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways
    • Dargemont, C. & Ossareh-Nazari, B. Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways. Biochim. Biophys. Acta 1823, 138-144 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 138-144
    • Dargemont, C.1    Ossareh-Nazari, B.2
  • 13
    • 84855188325 scopus 로고    scopus 로고
    • The Cdc48 machine in endoplasmic reticulum associated protein degradation
    • Wolf, D. H. & Stolz, A. The Cdc48 machine in endoplasmic reticulum associated protein degradation. Biochim. Biophys. Acta 1823, 117-124 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 117-124
    • Wolf, D.H.1    Stolz, A.2
  • 15
    • 84949254701 scopus 로고    scopus 로고
    • Origin and functional evolution of the Cdc48/p97/VCP AAA+ protein unfolding and remodeling machine
    • Barthelme, D. & Sauer, R. T. Origin and functional evolution of the Cdc48/p97/VCP AAA+ protein unfolding and remodeling machine. J. Mol. Biol. 428, 1861-1869 (2016).
    • (2016) J. Mol. Biol , vol.428 , pp. 1861-1869
    • Barthelme, D.1    Sauer, R.T.2
  • 16
    • 75349090585 scopus 로고    scopus 로고
    • ATP-bound form of the D1 AAA domain inhibits an essential function of Cdc48p/p97
    • Esaki, M. & Ogura, T. ATP-bound form of the D1 AAA domain inhibits an essential function of Cdc48p/p97. Biochem. cell Biol. 88, 109-117 (2010).
    • (2010) Biochem. Cell Biol , vol.88 , pp. 109-117
    • Esaki, M.1    Ogura, T.2
  • 17
    • 79955525976 scopus 로고    scopus 로고
    • Positive cooperativity of the p97 AAA ATPase is critical for essential functions
    • Nishikori, S., Esaki, M., Yamanaka, K., Sugimoto, S. & Ogura, T. Positive cooperativity of the p97 AAA ATPase is critical for essential functions. J. Biol. Chem. 286, 15815-15820 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 15815-15820
    • Nishikori, S.1    Esaki, M.2    Yamanaka, K.3    Sugimoto, S.4    Ogura, T.5
  • 18
    • 33847711447 scopus 로고    scopus 로고
    • Mutations in p97/VCP induce unfolding activity
    • Rothballer, A., Tzvetkov, N. & Zwickl, P. Mutations in p97/VCP induce unfolding activity. FEBS Lett 581, 1197-1201 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 1197-1201
    • Rothballer, A.1    Tzvetkov, N.2    Zwickl, P.3
  • 19
    • 84874452437 scopus 로고    scopus 로고
    • Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase
    • Barthelme, D. & Sauer, R. T. Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase. Proc. Natl. Acad. Sci. USA 110, 3327-3332 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 3327-3332
    • Barthelme, D.1    Sauer, R.T.2
  • 20
    • 84876916040 scopus 로고    scopus 로고
    • Structural biology of the proteasome
    • Kish-Trier, E. & Hill, C. P. Structural biology of the proteasome. Annu. Rev. Biophys 42, 29-49 (2013).
    • (2013) Annu. Rev. Biophys , vol.42 , pp. 29-49
    • Kish-Trier, E.1    Hill, C.P.2
  • 21
    • 70449524302 scopus 로고    scopus 로고
    • A conserved unfoldase activity for the p97 AAA-ATPase in proteasomal degradation
    • Beskow, A. et al. A conserved unfoldase activity for the p97 AAA-ATPase in proteasomal degradation. J. Mol. Biol. 394, 732-746 (2009).
    • (2009) J. Mol. Biol , vol.394 , pp. 732-746
    • Beskow, A.1
  • 24
    • 80055087132 scopus 로고    scopus 로고
    • The general definition of the p97/valosin-containing protein (VCP)-interacting motif (VIM) delineates a new family of p97 cofactors
    • Stapf, C., Cartwright, E., Bycroft, M., Hofmann, K. & Buchberger, A. The general definition of the p97/valosin-containing protein (VCP)-interacting motif (VIM) delineates a new family of p97 cofactors. J. Biol. Chem. 286, 38670-38678 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 38670-38678
    • Stapf, C.1    Cartwright, E.2    Bycroft, M.3    Hofmann, K.4    Buchberger, A.5
  • 25
    • 84995400216 scopus 로고    scopus 로고
    • Cdc48 and Ubx1 participate in an inner nuclear membrane associated degradation pathway that governs the turnover of Asi1
    • Pantazopoulou, M., Boban, M., Foisner, R. & Ljungdahl, P. O. Cdc48 and Ubx1 participate in an inner nuclear membrane associated degradation pathway that governs the turnover of Asi1. J. Cell Sci. 3770-3780 (2016).
    • (2016) J. Cell Sci , pp. 3770-3780
    • Pantazopoulou, M.1    Boban, M.2    Foisner, R.3    Ljungdahl, P.O.4
  • 26
    • 79953152149 scopus 로고    scopus 로고
    • A Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasis
    • Tran, J. R., Tomsic, L. R. & Brodsky, J. L. A Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasis. J. Biol. Chem. 286, 5744-5755 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 5744-5755
    • Tran, J.R.1    Tomsic, L.R.2    Brodsky, J.L.3
  • 27
    • 84873909937 scopus 로고    scopus 로고
    • The budding yeast Cdc48Shp1 complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7)
    • Böhm, S. & Buchberger, A. The budding yeast Cdc48Shp1 complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7). PLoS One 8, 22-24 (2013).
    • (2013) PLoS One , vol.8 , pp. 22-24
    • Böhm, S.1    Buchberger, A.2
  • 28
    • 4444320698 scopus 로고    scopus 로고
    • A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
    • Medicherla, B., Kostova, Z., Schaefer, A. & Wolf, D. H. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep. 5, 692-697 (2004).
    • (2004) EMBO Rep , vol.5 , pp. 692-697
    • Medicherla, B.1    Kostova, Z.2    Schaefer, A.3    Wolf, D.H.4
  • 29
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly, H. et al. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84 (2005).
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1
  • 30
    • 80051998695 scopus 로고    scopus 로고
    • The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23
    • Baek, G. H., Kim, I. & Rao, H. The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23. Proc. Natl. Acad. Sci. USA. 108, 13558-13563 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 13558-13563
    • Baek, G.H.1    Kim, I.2    Rao, H.3
  • 31
    • 79953771687 scopus 로고    scopus 로고
    • Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding
    • Böhm, S., Lamberti, G., Fernández-Sáiz, V., Stapf, C. & Buchberger, A. Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding. Mol. Cell. Biol. 31, 1528-1539 (2011).
    • (2011) Mol. Cell. Biol , vol.31 , pp. 1528-1539
    • Böhm, S.1    Lamberti, G.2    Fernández-Sáiz, V.3    Stapf, C.4    Buchberger, A.5
  • 32
    • 0031932987 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p
    • Madeo, F., Schlauer, J., Zischka, H., Mecke, D. & Fröhlich, K.-U. Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p. Mol. Biol. Cell 9, 131-141 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 131-141
    • Madeo, F.1    Schlauer, J.2    Zischka, H.3    Mecke, D.4    Fröhlich, K.-U.5
  • 33
    • 0027457543 scopus 로고
    • The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis
    • Hilt, W., Enenkel, C., Gruhler, A., Singer, T. & Wolf, D. H. The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis. J. Biol. Chem. 268, 3479-3486 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 3479-3486
    • Hilt, W.1    Enenkel, C.2    Gruhler, A.3    Singer, T.4    Wolf, D.H.5
  • 34
    • 77954748535 scopus 로고    scopus 로고
    • A chemical tool box defines mitotic and interphase roles for Mps1 kinase
    • Lan, W. & Cleveland, D. W. A chemical tool box defines mitotic and interphase roles for Mps1 kinase. J. Cell Biol. 190, 21-24 (2010).
    • (2010) J. Cell Biol , vol.190 , pp. 21-24
    • Lan, W.1    Cleveland, D.W.2
  • 36
    • 83755162358 scopus 로고    scopus 로고
    • Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase
    • Liu, C. et al. Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase. J. Biol. Chem. 286, 43660-43667 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 43660-43667
    • Liu, C.1
  • 37
    • 84964314276 scopus 로고    scopus 로고
    • Inducible tightly regulated and growth condition-independent transcription factor in Saccharomyces cerevisiae
    • Ottoz, D. S. M., Rudolf, F. & Stelling, J. Inducible, tightly regulated and growth condition-independent transcription factor in Saccharomyces cerevisiae. Nucleic Acids Res 42, e130 (2014).
    • (2014) Nucleic Acids Res , vol.42 , pp. e130
    • Ottoz, D.S.M.1    Rudolf, F.2    Stelling, J.3
  • 38
    • 1642343784 scopus 로고    scopus 로고
    • Phylogenetic analysis of AAA proteins
    • Frickey, T. & Lupas, A. N. Phylogenetic analysis of AAA proteins. J. Struct. Biol. 146, 2-10 (2004).
    • (2004) J. Struct. Biol , vol.146 , pp. 2-10
    • Frickey, T.1    Lupas, A.N.2
  • 39
    • 33646535590 scopus 로고    scopus 로고
    • Central pore residues mediate the p97/VCP activity required for ERAD
    • DeLaBarre, B., Christianson, J. C., Kopito, R. R. & Brunger, A. T. Central pore residues mediate the p97/VCP activity required for ERAD. Mol. Cell 22, 451-462 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 451-462
    • DeLaBarre, B.1    Christianson, J.C.2    Kopito, R.R.3    Brunger, A.T.4
  • 40
    • 0037423187 scopus 로고    scopus 로고
    • ATPase activity of p97-valosin-containing protein (VCP): D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity
    • Song, C., Wang, Q. & Li, C.-C. H. ATPase activity of p97-valosin-containing protein (VCP): D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity. J. Biol. Chem. 278, 3648-3655 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 3648-3655
    • Song, C.1    Wang, Q.2    Li, C.-C.H.3
  • 41
    • 30044443816 scopus 로고    scopus 로고
    • VAT, the Thermoplasma Homolog of Mammalian p97/VCP, Is an N Domain-regulated Protein Unfoldase
    • Gerega, A. et al. VAT, the Thermoplasma Homolog of Mammalian p97/VCP, Is an N Domain-regulated Protein Unfoldase. J. Biol. Chem. 280, 42856-42862 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 42856-42862
    • Gerega, A.1
  • 42
    • 85018732290 scopus 로고    scopus 로고
    • Molecular Mechanism of Substrate Processing by the Cdc48 ATPase Complex
    • Bodnar, N. O. & Rapoport, T. A. Molecular Mechanism of Substrate Processing by the Cdc48 ATPase Complex. Cell 169, 722-735. e9 (2017).
    • (2017) Cell , vol.169 , pp. 722-722e9
    • Bodnar, N.O.1    Rapoport, T.A.2
  • 43
    • 84865094127 scopus 로고    scopus 로고
    • Identification of the Cdc48·20S proteasome as an ancient AAA+ proteolytic machine
    • Barthelme, D. & Sauer, R. T. Identification of the Cdc48·20S proteasome as an ancient AAA+ proteolytic machine. Science 337, 843-846 (2012).
    • (2012) Science , vol.337 , pp. 843-846
    • Barthelme, D.1    Sauer, R.T.2
  • 44
    • 3042764201 scopus 로고    scopus 로고
    • Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis
    • Kim, I., Mi, K. & Rao, H. Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol. Biol. Cell 15, 3357-65 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3357-3365
    • Kim, I.1    Mi, K.2    Rao, H.3
  • 45
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S. & Hieter, P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27 (1989).
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 47
    • 0031818471 scopus 로고    scopus 로고
    • Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe
    • Bähler, J. et al. Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe. Yeast 14, 943-951 (1998).
    • (1998) Yeast , vol.14 , pp. 943-951
    • Bähler, J.1
  • 48
    • 84864382366 scopus 로고    scopus 로고
    • Cdc48p/p97-mediated regulation of mitochondrial morphology is Vms1p-independent
    • Esaki, M. & Ogura, T. Cdc48p/p97-mediated regulation of mitochondrial morphology is Vms1p-independent. J. Struct. Biol. 179, 112-120 (2012).
    • (2012) J. Struct. Biol , vol.179 , pp. 112-120
    • Esaki, M.1    Ogura, T.2


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