Trafficking of Lyn through the Golgi caveolin involves the charged residues on αE and αI helices in the kinase domain

Journal of Cell Biology

Volumn 165, Issue 5, 2004, Pages 641-652

  Kasahara, Kousuke ^a   Nakayama, Yuji ^a   Ikeda, Kikuko ^a   Fukushima, Yuka ^a   Matsuda, Daisuke ^a   Horimoto, Shinya ^a   Yamaguchi, Naoto ^a  

^a CHIBA UNIVERSITY   (Japan)

Author keywords

FRAP; Intracellular localization; Open conformation; Secretory pathway; Src family tyrosine kinase

Indexed keywords

CAVEOLIN; PROTEIN KINASE LYN; PROTEIN TYROSINE KINASE;

ANIMAL CELL; ARTICLE; CATALYSIS; CELL MEMBRANE; CONTROLLED STUDY; ENZYME LOCALIZATION; ENZYME PHOSPHORYLATION; GOLGI COMPLEX; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; IMMUNOPRECIPITATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; TRANSPORT KINETICS; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; ASPARTIC ACID; CAVEOLAE; CAVEOLIN 1; CAVEOLINS; CELL MEMBRANE; COS CELLS; GLUTAMIC ACID; GOLGI APPARATUS; HELA CELLS; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; SRC-FAMILY KINASES;

ANIMALIA;

EID: 2942640590     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200403011     Document Type: Article

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