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Volumn 7, Issue 12, 2011, Pages 1500-1513

Atg16L2, a novel isoform of mammalian Atg16L that is not essential for canonical autophagy despite forming an Atg12-5-16L2 complex

Author keywords

Atg16L; Autophagosome; Autophagy; Coiled coil domain; LC3; Rab effector; Rab33 binding protein

Indexed keywords

AMINO ACID; ATG 16L1 PROTEIN; ATG12 PROTEIN; ATG16 PROTEIN; AUTOPHAGY PROTEIN 5; ISOPROTEIN; MEMBRANE PROTEIN; OLIGOMER; UNCLASSIFIED DRUG;

EID: 82855169504     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.7.12.18025     Document Type: Article
Times cited : (79)

References (41)
  • 1
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • PMID:11265251
    • Ohsumi Y. Molecular dissection of autophagy: two ubiquitin-like systems. Nat Rev Mol Cell Biol 2001; 2:211-6; PMID:11265251; http://dx.doi.org/10.1038/ 35056522
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 2
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • PMID:15068787
    • Levine B, Klionsky DJ. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell 2004; 6:463-77; PMID:15068787; http://dx.doi.org/10.1016/S1534-5807(04)00099-1
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 3
    • 47149103494 scopus 로고    scopus 로고
    • Toward unraveling membrane biogenesis in mammalian autophagy
    • PMID:18472412
    • Yoshimori T, Noda T. Toward unraveling membrane biogenesis in mammalian autophagy. Curr Opin Cell Biol 2008; 20:401-7; PMID:18472412; http://dx.doi.org/10.1016/j.ceb.2008.03.010
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 401-407
    • Yoshimori, T.1    Noda, T.2
  • 4
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • PMID:18305538
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451:1069-75; PMID:18305538; http://dx.doi.org/10.1038/nature06639
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 5
    • 34248139628 scopus 로고    scopus 로고
    • Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae
    • PMID:17382324
    • Suzuki K, Ohsumi Y. Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae. FEBS Lett 2007; 581:2156-61; PMID:17382324; http://dx.doi.org/10.1016/j.febslet.2007.01.096
    • (2007) FEBS Lett , vol.581 , pp. 2156-2161
    • Suzuki, K.1    Ohsumi, Y.2
  • 6
    • 0038325675 scopus 로고    scopus 로고
    • Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate
    • PMID:12665549
    • Mizushima N, Kuma A, Kobayashi Y, Yamamoto A, Matsubae M, Takao T, et al. Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J Cell Sci 2003; 116:1679-88; PMID:12665549; http://dx.doi.org/10.1242/jcs.00381
    • (2003) J Cell Sci , vol.116 , pp. 1679-1688
    • Mizushima, N.1    Kuma, A.2    Kobayashi, Y.3    Yamamoto, A.4    Matsubae, M.5    Takao, T.6
  • 7
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • PMID:15525940
    • Kuma A, Hatano M, Matsui M, Yamamoto A, Nakaya H, Yoshimori T, et al. The role of autophagy during the early neonatal starvation period. Nature 2004; 432:1032-6; PMID:15525940; http://dx.doi.org/10.1038/nature03029
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1    Hatano, M.2    Matsui, M.3    Yamamoto, A.4    Nakaya, H.5    Yoshimori, T.6
  • 8
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1â production
    • PMID:18849965
    • Saitoh T, Fujita N, Jang MH, Uematsu S, Yang BG, Satoh T, et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1â production. Nature 2008; 456:264-8; PMID:18849965; http://dx.doi.org/10.1038/nature07383
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1    Fujita, N.2    Jang, M.H.3    Uematsu, S.4    Yang, B.G.5    Satoh, T.6
  • 9
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • PMID: 17986448
    • Hanada T, Noda NN, Satomi Y, Ichimura Y, Fujioka Y, Takao T, et al. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem 2007; 282:37298-302; PMID: 17986448; http://dx.doi.org/ 10.1074/jbc.C700195200
    • (2007) J Biol Chem , vol.282 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3    Ichimura, Y.4    Fujioka, Y.5    Takao, T.6
  • 10
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • PMID:18321988
    • Fujita N, Itoh T, Omori H, Fukuda M, Noda T, Yoshimori T. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol Biol Cell 2008; 19:2092-100; PMID:18321988; http://dx.doi.org/10. 1091/mbc.E07-12-1257
    • (2008) Mol Biol Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 11
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homolog of yeast Apg8p, is localized in autophagosome membranes after processing
    • PMID: 11060023
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, et al. LC3, a mammalian homolog of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19:5720-8; PMID: 11060023; http://dx.doi.org/10. 1093/emboj/19.21.5720
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6
  • 12
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion
    • PMID:17632063
    • Nakatogawa H, Ichimura Y, Ohsumi Y. Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell 2007; 130:165-78; PMID:17632063; 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
  • 13
    • 33846627302 scopus 로고    scopus 로고
    • A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1
    • PMID:17200669
    • Hampe J, Franke A, Rosenstiel P, Till A, Teuber M, Huse K, et al. A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1. Nat Genet 2007; 39:207-11; PMID:17200669; http://dx.doi.org/10.1038/ng1954
    • (2007) Nat Genet , vol.39 , pp. 207-211
    • Hampe, J.1    Franke, A.2    Rosenstiel, P.3    Till, A.4    Teuber, M.5    Huse, K.6
  • 14
    • 34247554965 scopus 로고    scopus 로고
    • Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis
    • PMID:17435756
    • Rioux JD, Xavier RJ, Taylor KD, Silverberg MS, Goyette P, Huett A, et al. Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis. Nat Genet 2007; 39:596-604; PMID:17435756; http://dx.doi.org/10.1038/ng2032
    • (2007) Nat Genet , vol.39 , pp. 596-604
    • Rioux, J.D.1    Xavier, R.J.2    Taylor, K.D.3    Silverberg, M.S.4    Goyette, P.5    Huett, A.6
  • 15
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • PMID: 18849966
    • Cadwell K, Liu JY, Brown SL, Miyoshi H, Loh J, Lennerz JK, et al. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature 2008; 456:259-63; PMID: 18849966; http://dx.doi.org/10. 1038/nature07416
    • (2008) Nature , vol.456 , pp. 259-263
    • Cadwell, K.1    Liu, J.Y.2    Brown, S.L.3    Miyoshi, H.4    Loh, J.5    Lennerz, J.K.6
  • 16
    • 50249098491 scopus 로고    scopus 로고
    • Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation
    • PMID: 18448665
    • Itoh T, Fujita N, Kanno E, Yamamoto A, Yoshimori T, Fukuda M. Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol Biol Cell 2008; 19:2916-25; PMID: 18448665; http://dx.doi.org/10.1091/mbc.E07-12-1231
    • (2008) Mol Biol Cell , vol.19 , pp. 2916-2925
    • Itoh, T.1    Fujita, N.2    Kanno, E.3    Yamamoto, A.4    Yoshimori, T.5    Fukuda, M.6
  • 17
    • 0035575616 scopus 로고    scopus 로고
    • Rab GTPases: Specifying and deciphering organelle identity and function
    • PMID:11719054
    • Pfeffer SR. Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol 2001; 11:487-91; PMID:11719054; http://dx.doi.org/10.1016/S0962-8924(01)02147-X
    • (2001) Trends Cell Biol , vol.11 , pp. 487-491
    • Pfeffer, S.R.1
  • 18
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • PMID:11252952
    • Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001; 2:107-17; PMID:11252952; http://dx.doi.org/10.1038/35052055
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 19
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: Achieving specificity in membrane traffic
    • PMID: 16882731
    • Grosshans BL, Ortiz D, Novick P. Rabs and their effectors: achieving specificity in membrane traffic. Proc Natl Acad Sci USA 2006; 103:11821-7; PMID: 16882731; http://dx.doi.org/10.1073/pnas.0601617103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 21
    • 50249131810 scopus 로고    scopus 로고
    • Direct link between Atg protein and small GTPase Rab: Atg16L functions as a potential Rab33 effector in mammals
    • PMID:18670194
    • Fukuda M, Itoh T. Direct link between Atg protein and small GTPase Rab: Atg16L functions as a potential Rab33 effector in mammals. Autophagy 2008; 4:824-6; PMID:18670194
    • (2008) Autophagy , vol.4 , pp. 824-826
    • Fukuda, M.1    Itoh, T.2
  • 22
    • 70450248450 scopus 로고    scopus 로고
    • Differential involvement of Atg16L1 in Crohn disease and canonical autophagy: Analysis of the organization of the Atg16L1 complex in fibroblasts
    • PMID:19783656
    • Fujita N, Saitoh T, Kageyama S, Akira S, Noda T, Yoshimori T. Differential involvement of Atg16L1 in Crohn disease and canonical autophagy: analysis of the organization of the Atg16L1 complex in fibroblasts. J Biol Chem 2009; 284:32602-9; PMID:19783656; http://dx.doi.org/10.1074/jbc.M109.037671
    • (2009) J Biol Chem , vol.284 , pp. 32602-32609
    • Fujita, N.1    Saitoh, T.2    Kageyama, S.3    Akira, S.4    Noda, T.5    Yoshimori, T.6
  • 23
    • 74049140368 scopus 로고    scopus 로고
    • Dimeric coiled-coil structure of Saccharomyces cerevisiae ATG16 and its functional significance in autophagy
    • PMID:19889643
    • Fujioka Y, Noda NN, Nakatogawa H, Ohsumi Y, Inagaki F. Dimeric coiled-coil structure of Saccharomyces cerevisiae ATG16 and its functional significance in autophagy. J Biol Chem 2010; 285:1508-15; PMID:19889643; http://dx.doi.org/10.1074/jbc.M109.053520
    • (2010) J Biol Chem , vol.285 , pp. 1508-1515
    • Fujioka, Y.1    Noda, N.N.2    Nakatogawa, H.3    Ohsumi, Y.4    Inagaki, F.5
  • 24
    • 46749156739 scopus 로고    scopus 로고
    • Large scale screening for novel Rab effectors reveals unexpected broad Rab binding specificity
    • PMID:18256213
    • Fukuda M, Kanno E, Ishibashi K, Itoh T. Large scale screening for novel Rab effectors reveals unexpected broad Rab binding specificity. Mol Cell Proteomics 2008; 7:1031-42; PMID:18256213; http://dx.doi.org/10.1074/mcp. M700569-MCP200
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1031-1042
    • Fukuda, M.1    Kanno, E.2    Ishibashi, K.3    Itoh, T.4
  • 25
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • PMID: 18188003
    • Klionsky DJ, Abeliovich H, Agostinis P, Agrawal DK, Aliev G, Askew DS, et al. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 2008; 4:151-75; PMID: 18188003
    • (2008) Autophagy , vol.4 , pp. 151-175
    • Klionsky, D.J.1    Abeliovich, H.2    Agostinis, P.3    Agrawal, D.K.4    Aliev, G.5    Askew, D.S.6
  • 26
    • 33646204392 scopus 로고    scopus 로고
    • Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size
    • PMID:16647067
    • Hosokawa N, Hara Y, Mizushima N. Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size. FEBS Lett 2006; 580:2623-9; PMID:16647067; http://dx.doi.org/10.1016/j. febslet.2006.04.008
    • (2006) FEBS Lett , vol.580 , pp. 2623-2629
    • Hosokawa, N.1    Hara, Y.2    Mizushima, N.3
  • 27
    • 77954898129 scopus 로고    scopus 로고
    • A genome-wide siRNA screen reveals multiple mTORC1 independent signaling pathways regulating autophagy under normal nutritional conditions
    • PMID:20627085
    • Lipinski MM, Hoffman G, Ng A, Zhou W, Py BF, Hsu E, et al. A genome-wide siRNA screen reveals multiple mTORC1 independent signaling pathways regulating autophagy under normal nutritional conditions. Dev Cell 2010; 18:1041-52; PMID:20627085; http://dx.doi.org/10.1016/j.devcel.2010.05.005
    • (2010) Dev Cell , vol.18 , pp. 1041-1052
    • Lipinski, M.M.1    Hoffman, G.2    Ng, A.3    Zhou, W.4    Py, B.F.5    Hsu, E.6
  • 28
    • 79952422876 scopus 로고    scopus 로고
    • OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation
    • PMID:21383079
    • Itoh T, Kanno E, Uemura T, Waguri S, Fukuda M. OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation. J Cell Biol 2011; 192:839-53; PMID:21383079; http://dx.doi.org/10.1083/jcb.201008107
    • (2011) J Cell Biol , vol.192 , pp. 839-853
    • Itoh, T.1    Kanno, E.2    Uemura, T.3    Waguri, S.4    Fukuda, M.5
  • 29
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • PMID:18006683
    • Mizushima N. Autophagy: process and function. Genes Dev 2007; 21:2861-73; PMID:18006683; http://dx.doi.org/10.1101/gad.1599207
    • (2007) Genes Dev , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 30
    • 0033615526 scopus 로고    scopus 로고
    • A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane domain: Implications for distinct functions of the two isoforms
    • PMID: 10531344
    • Fukuda M, Mikoshiba K. A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane domain: implications for distinct functions of the two isoforms. J Biol Chem 1999; 274:31428-34; PMID: 10531344; http://dx.doi.org/10.1074/jbc.274.44.31428
    • (1999) J Biol Chem , vol.274 , pp. 31428-31434
    • Fukuda, M.1    Mikoshiba, K.2
  • 31
    • 0033615704 scopus 로고    scopus 로고
    • Conserved N-terminal cysteine motif is essential for homo- And heterodimer formation of synaptotagmins III, V, VI, and X
    • PMID: 10531343
    • Fukuda M, Kanno E, Mikoshiba K. Conserved N-terminal cysteine motif is essential for homo- and heterodimer formation of synaptotagmins III, V, VI, and X. J Biol Chem 1999; 274:31421-7; PMID: 10531343; http://dx.doi.org/10.1074/jbc. 274.44.31421
    • (1999) J Biol Chem , vol.274 , pp. 31421-31427
    • Fukuda, M.1    Kanno, E.2    Mikoshiba, K.3
  • 32
    • 0028859443 scopus 로고
    • Functional diversity of C2 domains of synaptotagmin family: Mutational analysis of inositol high polyphosphate binding domain
    • PMID:7592870
    • Fukuda M, Kojima T, Aruga J, Niinobe M, Mikoshiba K. Functional diversity of C2 domains of synaptotagmin family: mutational analysis of inositol high polyphosphate binding domain. J Biol Chem 1995; 270:26523-7; PMID:7592870
    • (1995) J Biol Chem , vol.270 , pp. 26523-26527
    • Fukuda, M.1    Kojima, T.2    Aruga, J.3    Niinobe, M.4    Mikoshiba, K.5
  • 33
    • 0034046944 scopus 로고    scopus 로고
    • Plat-E: An efficient and stable system for transient packaging of retroviruses
    • PMID:10871756
    • Morita S, Kojima T, Kitamura T. Plat-E: an efficient and stable system for transient packaging of retroviruses. Gene Ther 2000; 7:1063-6; PMID:10871756; http://dx.doi.org/10.1038/sj.gt.3301206
    • (2000) Gene Ther , vol.7 , pp. 1063-1066
    • Morita, S.1    Kojima, T.2    Kitamura, T.3
  • 34
    • 58149290220 scopus 로고    scopus 로고
    • An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure
    • PMID:18768752
    • Fujita N, Hayashi-Nishino M, Fukumoto H, Omori H, Yamamoto A, Noda T, et al. An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure. Mol Biol Cell 2008; 19:4651-9; PMID:18768752; http://dx.doi.org/10.1091/mbc.E08-03-0312
    • (2008) Mol Biol Cell , vol.19 , pp. 4651-4659
    • Fujita, N.1    Hayashi-Nishino, M.2    Fukumoto, H.3    Omori, H.4    Yamamoto, A.5    Noda, T.6
  • 35
    • 0034815867 scopus 로고    scopus 로고
    • Novel splicing isoforms of synaptotagmin-like proteins 2 and 3: Identification of the Slp homology domain
    • PMID: 11327731
    • Fukuda M, Saegusa C, Mikoshiba K. Novel splicing isoforms of synaptotagmin-like proteins 2 and 3: identification of the Slp homology domain. Biochem Biophys Res Commun 2001; 283:513-9; PMID: 11327731; http://dx.doi.org/ 10.1006/bbrc.2001.4803
    • (2001) Biochem Biophys Res Commun , vol.283 , pp. 513-519
    • Fukuda, M.1    Saegusa, C.2    Mikoshiba, K.3
  • 36
    • 28244460438 scopus 로고    scopus 로고
    • Analysis of the role of Rab27 effector Slp4-a/granuphilin-a in dense-core vesicle exocytosis
    • PMID:16473610
    • Fukuda M, Kanno E. Analysis of the role of Rab27 effector Slp4-a/granuphilin-a in dense-core vesicle exocytosis. Methods Enzymol 2005; 403:445-57; PMID:16473610; http://dx.doi.org/10.1016/S0076-6879(05)03039-9
    • (2005) Methods Enzymol , vol.403 , pp. 445-457
    • Fukuda, M.1    Kanno, E.2
  • 37
    • 28244452750 scopus 로고    scopus 로고
    • Identification and biochemical analysis of Slac2-c/MyRIP as a Rab27A-, myosin Va/VIIa-, and actin-binding protein
    • PMID:16473609
    • Kuroda TS, Fukuda M. Identification and biochemical analysis of Slac2-c/MyRIP as a Rab27A-, myosin Va/VIIa-, and actin-binding protein. Methods Enzymol 2005; 403:431-44; PMID:16473609; http://dx.doi.org/10.1016/S0076- 6879(05)03038-7
    • (2005) Methods Enzymol , vol.403 , pp. 431-444
    • Kuroda, T.S.1    Fukuda, M.2
  • 38
    • 28244484879 scopus 로고    scopus 로고
    • The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells
    • PMID: 16203731
    • Tsuboi T, Fukuda M. The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells. J Biol Chem 2005; 280:39253-9; PMID: 16203731; http://dx.doi.org/10.1074/ jbc.M507173200
    • (2005) J Biol Chem , vol.280 , pp. 39253-39259
    • Tsuboi, T.1    Fukuda, M.2
  • 39
    • 2542470460 scopus 로고    scopus 로고
    • Slac2-a/melanophilin contains multiple PEST-like sequences that are highly sensitive to proteolysis
    • PMID:15145961
    • Fukuda M, Itoh T. Slac2-a/melanophilin contains multiple PEST-like sequences that are highly sensitive to proteolysis. J Biol Chem 2004; 279:22314-21; PMID:15145961; http://dx.doi.org/10.1074/jbc.401791200
    • (2004) J Biol Chem , vol.279 , pp. 22314-22321
    • Fukuda, M.1    Itoh, T.2
  • 40
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • PMID:9396791
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools.Nucleic AcidsRes 1997; 25:4876-82; PMID:9396791; http://dx.doi.org/10.1093/nar/25.24.4876
    • (1997) Nucleic AcidsRes , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 41
    • 33747467878 scopus 로고    scopus 로고
    • Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing proteins based on their Rab-binding activity
    • PMID:16923123
    • Itoh T, Satoh M, Kanno E, Fukuda M. Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing proteins based on their Rab-binding activity. Genes Cells 2006; 11:1023-37; PMID:16923123; http://dx.doi.org/10. 1111/j.1365-2443.2006.00997.x
    • (2006) Genes Cells , vol.11 , pp. 1023-1037
    • Itoh, T.1    Satoh, M.2    Kanno, E.3    Fukuda, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.