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Volumn 207, Issue 1, 2014, Pages 91-105

Hrr25 triggers selective autophagy-related pathways by phosphorylating receptor proteins

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE; PROTEIN HRR25; RECEPTOR PROTEIN; UNCLASSIFIED DRUG; AMINOPEPTIDASE; APE1 PROTEIN, S CEREVISIAE; ATG11 PROTEIN, S CEREVISIAE; ATG19 PROTEIN, S CEREVISIAE; ATG36 PROTEIN, S CEREVISIAE; CASEIN KINASE I; CELL SURFACE RECEPTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HRR25 PROTEIN, S CEREVISIAE; MEMBRANE PROTEIN; PEX3 PROTEIN, S CEREVISIAE; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; SEC23 PROTEIN, S CEREVISIAE; VESICULAR TRANSPORT PROTEIN;

EID: 84908361088     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201402128     Document Type: Article
Times cited : (98)

References (53)
  • 1
    • 0015792521 scopus 로고
    • Processing of adenovirus 2-induced proteins
    • Anderson, C.W., P.R. Baum, and R.F. Gesteland. 1973. Processing of adenovirus 2-induced proteins. J. Virol. 12:241-252.
    • (1973) J. Virol , vol.12 , pp. 241-252
    • Anderson, C.W.1    Baum, P.R.2    Gesteland, R.F.3
  • 3
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C.B., A. Davies, G.J. Cost, E. Caputo, J. Li, P. Hieter, and J.D. Boeke. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast. 14:115-132. http://dx.doi.org/10.1002/ (SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2-2.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 5
    • 0026741994 scopus 로고
    • The budding yeast HRR25 gene product is a casein kinase I isoform
    • DeMaggio, A.J., R.A. Lindberg, T. Hunter, and M.F. Hoekstra. 1992. The budding yeast HRR25 gene product is a casein kinase I isoform. Proc. Natl. Acad. Sci. USA. 89:7008-7012. http://dx.doi.org/10.1073/pnas.89.15.7008.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7008-7012
    • DeMaggio, A.J.1    Lindberg, R.A.2    Hunter, T.3    Hoekstra, M.F.4
  • 6
    • 67649607465 scopus 로고    scopus 로고
    • Autophagy, immunity, and microbial adaptations
    • Deretic, V., and B. Levine. 2009. Autophagy, immunity, and microbial adaptations. Cell Host Microbe. 5:527-549. http://dx.doi.org/10.1016/ j.chom.2009.05.016.
    • (2009) Cell Host Microbe , vol.5 , pp. 527-549
    • Deretic, V.1    Levine, B.2
  • 7
    • 42049094041 scopus 로고    scopus 로고
    • PpAtg30 tags peroxisomes for turnover by selective autophagy
    • Farré, J.C., R. Manjithaya, R.D. Mathewson, and S. Subramani. 2008. PpAtg30 tags peroxisomes for turnover by selective autophagy. Dev. Cell. 14:365-376. http://dx.doi.org/10.1016/j.devcel.2007.12.011.
    • (2008) Dev. Cell , vol.14 , pp. 365-376
    • Farré, J.C.1    Manjithaya, R.2    Mathewson, R.D.3    Subramani, S.4
  • 8
    • 84877579321 scopus 로고    scopus 로고
    • Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11
    • Farré, J.C., A. Burkenroad, S.F. Burnett, and S. Subramani. 2013. Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11. EMBO Rep. 14:441-449. http://dx.doi.org/10.1038/embor.2013.40.
    • (2013) EMBO Rep , vol.14 , pp. 441-449
    • Farré, J.C.1    Burkenroad, A.2    Burnett, S.F.3    Subramani, S.4
  • 9
    • 0025800543 scopus 로고
    • HRR25, a putative protein kinase from budding yeast: association with repair of damaged DNA
    • Hoekstra, M.F., R.M. Liskay, A.C. Ou, A.J. DeMaggio, D.G. Burbee, and F. Heffron. 1991. HRR25, a putative protein kinase from budding yeast: association with repair of damaged DNA. Science. 253:1031-1034. http://dx.doi.org/10.1126/science.1887218.
    • (1991) Science , vol.253 , pp. 1031-1034
    • Hoekstra, M.F.1    Liskay, R.M.2    Ou, A.C.3    DeMaggio, A.J.4    Burbee, D.G.5    Heffron, F.6
  • 10
    • 0035827541 scopus 로고    scopus 로고
    • Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae
    • Hutchins, M.U., and D.J. Klionsky. 2001. Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae. J. Biol. Chem. 276:20491-20498. http://dx.doi.org/10.1074/jbc.M101150200.
    • (2001) J. Biol. Chem , vol.276 , pp. 20491-20498
    • Hutchins, M.U.1    Klionsky, D.J.2
  • 11
    • 0035192612 scopus 로고    scopus 로고
    • Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion
    • Ishihara, N., M. Hamasaki, S. Yokota, K. Suzuki, Y. Kamada, A. Kihara, T. Yoshimori, T. Noda, and Y. Ohsumi. 2001. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol. Biol. Cell. 12:3690-3702. http://dx.doi.org/10.1091/mbc.12.11.3690.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3690-3702
    • Ishihara, N.1    Hamasaki, M.2    Yokota, S.3    Suzuki, K.4    Kamada, Y.5    Kihara, A.6    Yoshimori, T.7    Noda, T.8    Ohsumi, Y.9
  • 12
  • 13
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen, T., and T. Lamark. 2011. Selective autophagy mediated by autophagic adapter proteins. Autophagy. 7:279-296. http://dx.doi.org/10.4161/ auto.7.3.14487.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 15
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki, T., K. Wang, Y. Cao, M. Baba, and D.J. Klionsky. 2009b. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev. Cell. 17:98-109. http://dx.doi.org/10.1016/j.devcel.2009.06.014.
    • (2009) Dev. Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 17
    • 0030997923 scopus 로고    scopus 로고
    • Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway
    • Kim, J., S.V. Scott, M.N. Oda, and D.J. Klionsky. 1997. Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway. J. Cell Biol. 137:609-618. http://dx.doi.org/10.1083/jcb.137.3.609.
    • (1997) J. Cell Biol , vol.137 , pp. 609-618
    • Kim, J.1    Scott, S.V.2    Oda, M.N.3    Klionsky, D.J.4
  • 18
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., D.G. McEwan, I. Novak, and I. Dikic. 2009. A role for ubiquitin in selective autophagy. Mol. Cell. 34:259-269. http://dx.doi.org/ 10.1016/j.molcel.2009.04.026.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 20
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • Kraft, C., A. Deplazes, M. Sohrmann, and M. Peter. 2008. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell Biol. 10:602-610. http://dx.doi.org/10.1038/ncb1723.
    • (2008) Nat. Cell Biol , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 21
    • 84887132374 scopus 로고    scopus 로고
    • Arginine methylation modulates autophagic degradation of PGL granules in C
    • Li, S., P. Yang, E. Tian, and H. Zhang. 2013. Arginine methylation modulates autophagic degradation of PGL granules in C. elegans. Mol. Cell. 52:421-433. http://dx.doi.org/10.1016/j.molcel.2013.09.014.
    • (2013) elegans. Mol. Cell , vol.52 , pp. 421-433
    • Li, S.1    Yang, P.2    Tian, E.3    Zhang, H.4
  • 22
    • 84862789618 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
    • Liu, L., D. Feng, G. Chen, M. Chen, Q. Zheng, P. Song, Q. Ma, C. Zhu, R. Wang, W. Qi, et al. 2012. Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nat. Cell Biol. 14:177-185. http://dx.doi.org/10.1038/ncb2422.
    • (2012) Nat. Cell Biol , vol.14 , pp. 177-185
    • Liu, L.1    Feng, D.2    Chen, G.3    Chen, M.4    Zheng, Q.5    Song, P.6    Ma, Q.7    Zhu, C.8    Wang, R.9    Qi, W.10
  • 23
    • 79955880405 scopus 로고    scopus 로고
    • Sequential interactions with Sec23 control the direction of vesicle traffic
    • Lord, C., D. Bhandari, S. Menon, M. Ghassemian, D. Nycz, J. Hay, P. Ghosh, and S. Ferro-Novick. 2011. Sequential interactions with Sec23 control the direction of vesicle traffic. Nature. 473:181-186. http://dx.doi.org/10.1038/nature09969.
    • (2011) Nature , vol.473 , pp. 181-186
    • Lord, C.1    Bhandari, D.2    Menon, S.3    Ghassemian, M.4    Nycz, D.5    Hay, J.6    Ghosh, P.7    Ferro-Novick, S.8
  • 24
    • 77950510302 scopus 로고    scopus 로고
    • The Cvt pathway as a model for selective autophagy
    • Lynch-Day, M.A., and D.J. Klionsky. 2010. The Cvt pathway as a model for selective autophagy. FEBS Lett. 584:1359-1366. http://dx.doi.org/10.1016/ j.febslet.2010.02.013.
    • (2010) FEBS Lett , vol.584 , pp. 1359-1366
    • Lynch-Day, M.A.1    Klionsky, D.J.2
  • 25
    • 82455172117 scopus 로고    scopus 로고
    • Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins
    • Matsumoto, G., K. Wada, M. Okuno, M. Kurosawa, and N. Nukina. 2011. Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. Mol. Cell. 44:279-289. http://dx.doi.org/10.1016/j.molcel.2011.07.039.
    • (2011) Mol. Cell , vol.44 , pp. 279-289
    • Matsumoto, G.1    Wada, K.2    Okuno, M.3    Kurosawa, M.4    Nukina, N.5
  • 26
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: renovation of cells and tissues
    • Mizushima, N., and M. Komatsu. 2011. Autophagy: renovation of cells and tissues. Cell. 147:728-741. http://dx.doi.org/10.1016/j.cell.2011.10.026.
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 27
    • 80054025654 scopus 로고    scopus 로고
    • The role of Atg proteins in autophagosome formation
    • Mizushima, N., T. Yoshimori, and Y. Ohsumi. 2011. The role of Atg proteins in autophagosome formation. Annu. Rev. Cell Dev. Biol. 27:107-132. http://dx.doi.org/10.1146/annurev-cellbio-092910-154005.
    • (2011) Annu. Rev. Cell Dev. Biol , vol.27 , pp. 107-132
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 28
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • Motley, A.M., J.M. Nuttall, and E.H. Hettema. 2012. Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J. 31:2852-2868. http://dx.doi.org/10.1038/emboj.2012.151.
    • (2012) EMBO J , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 29
    • 0033524921 scopus 로고    scopus 로고
    • The inactive form of a yeast casein kinase I suppresses the secretory defect of the sec12 mutant. Implication of negative regulation by the Hrr25 kinase in the vesicle budding from the endoplasmic reticulum
    • Murakami, A., K. Kimura, and A. Nakano. 1999. The inactive form of a yeast casein kinase I suppresses the secretory defect of the sec12 mutant. Implication of negative regulation by the Hrr25 kinase in the vesicle budding from the endoplasmic reticulum. J. Biol. Chem. 274:3804-3810. http://dx.doi.org/10.1074/jbc.274.6.3804.
    • (1999) J. Biol. Chem , vol.274 , pp. 3804-3810
    • Murakami, A.1    Kimura, K.2    Nakano, A.3
  • 30
    • 84858220413 scopus 로고    scopus 로고
    • SDS-PAGE techniques to study ubiquitin-like conjugation systems in yeast autophagy
    • Nakatogawa, H., and Y. Ohsumi. 2012. SDS-PAGE techniques to study ubiquitin-like conjugation systems in yeast autophagy. Methods Mol. Biol. 832:519-529. http://dx.doi.org/10.1007/978-1-61779-474-2_37.
    • (2012) Methods Mol. Biol , vol.832 , pp. 519-529
    • Nakatogawa, H.1    Ohsumi, Y.2
  • 31
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion
    • Nakatogawa, H., Y. Ichimura, and Y. Ohsumi. 2007. Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell. 130:165-178. http://dx.doi.org/10.1016/ j.cell.2007.05.021.
    • (2007) Cell , vol.130 , pp. 165-178
    • Nakatogawa, H.1    Ichimura, Y.2    Ohsumi, Y.3
  • 32
    • 67649467294 scopus 로고    scopus 로고
    • Dynamics and diversity in autophagy mechanisms: lessons from yeast
    • Nakatogawa, H., K. Suzuki, Y. Kamada, and Y. Ohsumi. 2009. Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat. Rev. Mol. Cell Biol. 10:458-467. http://dx.doi.org/10.1038/nrm2708.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 458-467
    • Nakatogawa, H.1    Suzuki, K.2    Kamada, Y.3    Ohsumi, Y.4
  • 33
    • 84857256919 scopus 로고    scopus 로고
    • Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome biogenesis
    • Nakatogawa, H., J. Ishii, E. Asai, and Y. Ohsumi. 2012. Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome biogenesis. Autophagy. 8:177-186. http://dx.doi.org/10.4161/auto.8.2.18373.
    • (2012) Autophagy , vol.8 , pp. 177-186
    • Nakatogawa, H.1    Ishii, J.2    Asai, E.3    Ohsumi, Y.4
  • 34
    • 73349085934 scopus 로고    scopus 로고
    • An auxin-based degron system for the rapid depletion of proteins in nonplant cells
    • Nishimura, K., T. Fukagawa, H. Takisawa, T. Kakimoto, and M. Kanemaki. 2009. An auxin-based degron system for the rapid depletion of proteins in nonplant cells. Nat. Methods. 6:917-922. http://dx.doi.org/10.1038/ nmeth.1401.
    • (2009) Nat. Methods , vol.6 , pp. 917-922
    • Nishimura, K.1    Fukagawa, T.2    Takisawa, H.3    Kakimoto, T.4    Kanemaki, M.5
  • 36
    • 0029036915 scopus 로고
    • Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae
    • Noda, T., A. Matsuura, Y. Wada, and Y. Ohsumi. 1995. Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 210:126-132. http://dx.doi.org/10.1006/bbrc.1995.1636.
    • (1995) Biochem. Biophys. Res. Commun , vol.210 , pp. 126-132
    • Noda, T.1    Matsuura, A.2    Wada, Y.3    Ohsumi, Y.4
  • 37
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto, K., N. Kondo-Okamoto, and Y. Ohsumi. 2009. Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev. Cell. 17:87-97. http://dx.doi.org/10.1016/j.devcel.2009.06.013.
    • (2009) Dev. Cell , vol.17 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 38
    • 1942469479 scopus 로고    scopus 로고
    • Ald6p is a preferred target for autophagy in yeast, Saccharomyces cerevisiae
    • Onodera, J., and Y. Ohsumi. 2004. Ald6p is a preferred target for autophagy in yeast, Saccharomyces cerevisiae. J. Biol. Chem. 279:16071-16076. http://dx.doi.org/10.1074/jbc.M312706200.
    • (2004) J. Biol. Chem , vol.279 , pp. 16071-16076
    • Onodera, J.1    Ohsumi, Y.2
  • 41
    • 33745228890 scopus 로고    scopus 로고
    • Hrr25-dependent phosphorylation state regulates organization of the pre-40S subunit
    • Schäfer, T., B. Maco, E. Petfalski, D. Tollervey, B. Böttcher, U. Aebi, and E. Hurt. 2006. Hrr25-dependent phosphorylation state regulates organization of the pre-40S subunit. Nature. 441:651-655. http://dx.doi.org/10.1038/nature04840.
    • (2006) Nature , vol.441 , pp. 651-655
    • Schäfer, T.1    Maco, B.2    Petfalski, E.3    Tollervey, D.4    Böttcher, B.5    Aebi, U.6    Hurt, E.7
  • 42
    • 0034964443 scopus 로고    scopus 로고
    • Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway
    • Scott, S.V., J. Guan, M.U. Hutchins, J. Kim, and D.J. Klionsky. 2001. Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway. Mol. Cell. 7:1131-1141. http://dx.doi.org/10.1016/S1097-2765(01)00263-5.
    • (2001) Mol. Cell , vol.7 , pp. 1131-1141
    • Scott, S.V.1    Guan, J.2    Hutchins, M.U.3    Kim, J.4    Klionsky, D.J.5
  • 43
    • 3142677196 scopus 로고    scopus 로고
    • Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway
    • Shintani, T., and D.J. Klionsky. 2004. Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway. J. Biol. Chem. 279:29889-29894. http://dx.doi.org/10.1074/jbc.M404399200.
    • (2004) J. Biol. Chem , vol.279 , pp. 29889-29894
    • Shintani, T.1    Klionsky, D.J.2
  • 44
    • 0036901104 scopus 로고    scopus 로고
    • Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway
    • Shintani, T., W.P. Huang, P.E. Stromhaug, and D.J. Klionsky. 2002. Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway. Dev. Cell. 3:825-837. http://dx.doi.org/10.1016/S1534-5807(02)00373-8.
    • (2002) Dev. Cell , vol.3 , pp. 825-837
    • Shintani, T.1    Huang, W.P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 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., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 46
    • 3342951135 scopus 로고    scopus 로고
    • Atg21 is a phosphoinositide binding protein required for efficient lipidation and localization of Atg8 during uptake of aminopeptidase I by selective autophagy
    • Strømhaug, P.E., F. Reggiori, J. Guan, C.W. Wang, and D.J. Klionsky. 2004. Atg21 is a phosphoinositide binding protein required for efficient lipidation and localization of Atg8 during uptake of aminopeptidase I by selective autophagy. Mol. Biol. Cell. 15:3553-3566. http://dx.doi.org/ 10.1091/mbc.E04-02-0147.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3553-3566
    • Strømhaug, P.E.1    Reggiori, F.2    Guan, J.3    Wang, C.W.4    Klionsky, D.J.5
  • 47
    • 84871002139 scopus 로고    scopus 로고
    • Selective autophagy in budding yeast
    • Suzuki, K. 2013. Selective autophagy in budding yeast. Cell Death Differ. 20:43-48. http://dx.doi.org/10.1038/cdd.2012.73.
    • (2013) Cell Death Differ , vol.20 , pp. 43-48
    • Suzuki, K.1
  • 48
    • 0035503594 scopus 로고    scopus 로고
    • The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
    • Suzuki, K., T. Kirisako, Y. Kamada, N. Mizushima, T. Noda, and Y. Ohsumi. 2001. The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation. EMBO J. 20:5971-5981. http://dx.doi.org/10.1093/emboj/20.21.5971.
    • (2001) EMBO J , vol.20 , pp. 5971-5981
    • Suzuki, K.1    Kirisako, T.2    Kamada, Y.3    Mizushima, N.4    Noda, T.5    Ohsumi, Y.6
  • 49
    • 79959415069 scopus 로고    scopus 로고
    • Biogenesis and cargo selectivity of autophagosomes
    • Weidberg, H., E. Shvets, and Z. Elazar. 2011. Biogenesis and cargo selectivity of autophagosomes. Annu. Rev. Biochem. 80:125-156. http://dx.doi.org/10.1146/annurev-biochem-052709-094552.
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 125-156
    • Weidberg, H.1    Shvets, E.2    Elazar, Z.3
  • 51
    • 52649145895 scopus 로고    scopus 로고
    • GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy
    • Xue, Y., J. Ren, X. Gao, C. Jin, L. Wen, and X. Yao. 2008. GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy. Mol. Cell. Proteomics. 7:1598-1608. http://dx.doi.org/10.1074/mcp.M700574-MCP200.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1598-1608
    • Xue, Y.1    Ren, J.2    Gao, X.3    Jin, C.4    Wen, L.5    Yao, X.6
  • 52
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: a history of macroautophagy
    • Yang, Z., and D.J. Klionsky. 2010. Eaten alive: a history of macroautophagy. Nat. Cell Biol. 12:814-822. http://dx.doi.org/10.1038/ncb0910-814.
    • (2010) Nat. Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 53
    • 79953850827 scopus 로고    scopus 로고
    • Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiae
    • Yuga, M., K. Gomi, D.J. Klionsky, and T. Shintani. 2011. Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiae. J. Biol. Chem. 286:13704-13713. http://dx.doi.org/10.1074/jbc.M110.173906.
    • (2011) J. Biol. Chem , vol.286 , pp. 13704-13713
    • Yuga, M.1    Gomi, K.2    Klionsky, D.J.3    Shintani, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.