Selective transport of α-mannosidase by autophagic pathways: Structural basis for cargo recognition by Atg19 and Atg34

Journal of Biological Chemistry

Volumn 285, Issue 39, 2010, Pages 30026-30033

  Watanabe, Yasunori ^a   Noda, Nobuo N ^a   Kumeta, Hiroyuki ^a   Suzuki, Kuninori ^b   Ohsumi, Yoshinori ^b   Inagaki, Fuyuhiko ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE I; AUTOPHAGY; BINDING DOMAIN; C-TERMINAL DOMAINS; C-TERMINAL REGIONS; IN-VITRO; MANNOSIDASE; MOLECULAR MECHANISM; MUTATIONAL ANALYSIS; NMR SPECTROSCOPY; PARALOGS; PULLDOWN ASSAYS; SELECTIVE TRANSPORT; SOLUTION STRUCTURES; STARVATION CONDITIONS; STRUCTURAL BASIS; YEAST SACCHAROMYCES CEREVISIAE;

CYTOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PLANTS (BOTANY);

YEAST;

ALPHA MANNOSIDASE; IMMUNOGLOBULIN; PROTEIN ATG19; PROTEIN ATG34; RECEPTOR PROTEIN; UNCLASSIFIED DRUG; AMINOPEPTIDASE; APE1 PROTEIN, S CEREVISIAE; ATG11 PROTEIN, S CEREVISIAE; ATG19 PROTEIN, S CEREVISIAE; ATG8 PROTEIN, S CEREVISIAE; CELL SURFACE RECEPTOR; MICROTUBULE ASSOCIATED PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; VESICULAR TRANSPORT PROTEIN;

ARTICLE; AUTOPHAGY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; IN VITRO STUDY; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; CELL VACUOLE; CHEMISTRY; GENETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE;

ALPHA-MANNOSIDASE; AMINOPEPTIDASES; AUTOPHAGY; MICROTUBULE-ASSOCIATED PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECEPTORS, CELL SURFACE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; VACUOLES; VESICULAR TRANSPORT PROTEINS;

SACCHAROMYCES CEREVISIAE;

EID: 77956913181     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.143545     Document Type: Article

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