FLCN, a novel autophagy component, interacts with GABARAP and is regulated by ULK1 phosphorylation

Autophagy

Volumn 10, Issue 10, 2014, Pages 1749-1760

  Dunlop, Elaine A ^a   Seifan, Sara ^a   Claessens, Tijs ^a,b   Behrends, Christian ^c   Kamps, Miriam A F ^b   Rozycka, Ewelina ^d   Kemp, Alain J ^e   Nookala, Ravi K ^f   Blenis, John ^g   Coull, Barry J ^b   Murray, James T ^d,h   Van Steensel, Maurice A M ^b,i   Wilkinson, Simon ^e   Tee, Andrew R ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

^b MAASTRICHT UNIVERSITY   (Netherlands)

^c GOETHE UNIVERSITY MEDICAL SCHOOL   (Germany)

^d QUEEN'S UNIVERSITY BELFAST   (United Kingdom)

^e UNIVERSITY OF EDINBURGH   (United Kingdom)

^f UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^g HARVARD MEDICAL SCHOOL   (United States)

^h TRINITY COLLEGE DUBLIN   (Ireland)

ⁱ INSTITUTE OF MEDICAL BIOLOGY   (Singapore)

Author keywords

Autophagy; BHD; FLCN; GABARAP; MAP1LC3B; SQSTM1; ULK1

Indexed keywords

ESTRONE; FOLLICULIN INTERACTING PROTEIN 1; FOLLICULIN INTERACTING PROTEIN 2; GABA A RECEPTOR ASSOCIATED PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 1 LIGHT CHAIN 3; PEPTIDES AND PROTEINS; PROTEIN ULK1; SEQUESTOME 1; UNCLASSIFIED DRUG; CARRIER PROTEIN; FNIP1 PROTEIN, HUMAN; FNIP2 PROTEIN, HUMAN; GABARAP PROTEIN, HUMAN; MICROTUBULE ASSOCIATED PROTEIN; PROTEIN BINDING; PROTEIN SERINE THREONINE KINASE; SIGNAL PEPTIDE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SQSTM1 PROTEIN, HUMAN; ULK1 PROTEIN, HUMAN;

ARTICLE; AUTOPHAGY; COMPLEX FORMATION; CONTROLLED STUDY; HUMAN; HUMAN CELL; HUMAN TISSUE; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; ANIMAL; BIRT HOGG DUBE SYNDROME; CHEMISTRY; DEFICIENCY; METABOLISM; MOLECULAR GENETICS; MOUSE; PATHOLOGY; PHOSPHORYLATION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; ANIMALS; AUTOPHAGY; BIRT-HOGG-DUBE SYNDROME; CARRIER PROTEINS; ESTRONE; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MICE; MICROTUBULE-ASSOCIATED PROTEINS; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN-SERINE-THREONINE KINASES;

EID: 84907887033     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.29640     Document Type: Article

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