Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners

Autophagy

Volumn 11, Issue 1, 2015, Pages 75-87

  Kim, Jun Hoe ^a   Hong, Seung Beom ^a,c   Lee, Jae Keun ^a   Han, Sisu ^a   Roh, Kyung Hye ^a   Lee, Kyung Eun ^b   Kim, Yoon Ki ^a   Choi, Eui Ju ^a   Song, Hyun Kyu ^a  

^a Korea University   (South Korea)

^b Korea Institute of Science and Technology   (South Korea)

^c NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

ATG12; ATG16; ATG5; Crystal structure; Lysosome fusion; TECPR1

Indexed keywords

ATG5 ATG16N69 COMPLEX; ATG5 TECAIR COMPLEX; AUTOPHAGY PROTEIN 12; AUTOPHAGY PROTEIN 16L1; AUTOPHAGY PROTEIN 5; PROTEIN; TECTONIN BETA PROPELLER REPEAT CONTAINING 1; UNCLASSIFIED DRUG; ATG16L1 PROTEIN, HUMAN; ATG5 PROTEIN, HUMAN; CARRIER PROTEIN; MEMBRANE PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; MULTIPROTEIN COMPLEX; PROTEIN BINDING; TECPR1 PROTEIN, HUMAN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; AUTOPHAGOSOME; AUTOPHAGY PROTEIN 5 INTERACTING MOTIF; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CELL FUSION; CELL MATURATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; FEMALE; HUMAN; HUMAN CELL; LYSOSOME MEMBRANE; MOLECULAR INTERACTION; PH; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; AMINO ACID SEQUENCE; ANIMAL; AUTOPHAGY; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CHLOROCEBUS AETHIOPS; COS 1 CELL LINE; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; PHAGOSOME; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; ULTRASTRUCTURE;

EUKARYOTA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; AUTOPHAGY; CARRIER PROTEINS; CERCOPITHECUS AETHIOPS; COS CELLS; HUMANS; HYDROGEN-ION CONCENTRATION; MEMBRANE PROTEINS; MICROTUBULE-ASSOCIATED PROTEINS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; MUTATION; PHAGOSOMES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE;

EID: 84923329832     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/15548627.2014.984276     Document Type: Article

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