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LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation

LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation Research Article LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation 1 1,2, 3 1 Yukiko Kabeya , Noboru Mizushima *, Akitsugu Yamamoto , Satsuki Oshitani-Okamoto , 1 1,4,5,6,‡ Yoshinori Ohsumi and Tamotsu Yoshimori Department of Cell Biology, National Institute for Basic Biology, Myodaiji 38, Okazaki 444-8585, Japan PRESTO, Japan Science and Technology Agency, Honcho 4-1-8, Kawaguchi 332-0012, Japan Department of Bio-Science, Nagahama Institute of Bio-Science and Technology, Tamura 1266, Nagahama 526-0829, Japan Department of Cell Genetics, National Institute of Genetics, Yata 1111, Mishima 411-8540, Japan Department of Genetics, The Graduate University for Advanced Studies, Yata 1111, Mishima 411-8540, Japan CREST, Japan Science and Technology Agency, Honcho 4-1-8, Kawaguchi 332-0012, Japan *Present address: Department of Bioregulation and Metabolism, The Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan Author for correspondence (e-mail: tamyoshi@lab.nig.ac.jp) Accepted 30 January 2004 Journal of Cell Science 117, 2805-2812 Published by The Company of Biologists 2004 doi:10.1242/jcs.01131 Summary Rat LC3, a homologue of yeast Atg8 (Aut7/Apg8), localizes deconjugase, supporting the idea that LC3-II is LC3-PE. to autophagosomal membranes after post-translational Moreover, two other mammalian homologues of yeast Atg8, modifications. The C-terminal fragment of LC3 is cleaved g -aminobutyric-acid-type-A-receptor-associated protein http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Cell Science Unpaywall

LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation

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Unpaywall
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0021-9533
DOI
10.1242/jcs.01131
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Abstract

Research Article LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation 1 1,2, 3 1 Yukiko Kabeya , Noboru Mizushima *, Akitsugu Yamamoto , Satsuki Oshitani-Okamoto , 1 1,4,5,6,‡ Yoshinori Ohsumi and Tamotsu Yoshimori Department of Cell Biology, National Institute for Basic Biology, Myodaiji 38, Okazaki 444-8585, Japan PRESTO, Japan Science and Technology Agency, Honcho 4-1-8, Kawaguchi 332-0012, Japan Department of Bio-Science, Nagahama Institute of Bio-Science and Technology, Tamura 1266, Nagahama 526-0829, Japan Department of Cell Genetics, National Institute of Genetics, Yata 1111, Mishima 411-8540, Japan Department of Genetics, The Graduate University for Advanced Studies, Yata 1111, Mishima 411-8540, Japan CREST, Japan Science and Technology Agency, Honcho 4-1-8, Kawaguchi 332-0012, Japan *Present address: Department of Bioregulation and Metabolism, The Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan Author for correspondence (e-mail: tamyoshi@lab.nig.ac.jp) Accepted 30 January 2004 Journal of Cell Science 117, 2805-2812 Published by The Company of Biologists 2004 doi:10.1242/jcs.01131 Summary Rat LC3, a homologue of yeast Atg8 (Aut7/Apg8), localizes deconjugase, supporting the idea that LC3-II is LC3-PE. to autophagosomal membranes after post-translational Moreover, two other mammalian homologues of yeast Atg8, modifications. The C-terminal fragment of LC3 is cleaved g -aminobutyric-acid-type-A-receptor-associated protein

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Journal of Cell Science – Unpaywall

Published: Jun 1, 2004

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