The length of cargo-protein transmembrane segments drives secretory transport by facilitating cargo concentration in export domains

Journal of Cell Science

Volumn 122, Issue 11, 2009, Pages 1759-1767

  Dukhovny, Anna ^a   Yaffe, Yakey ^a   Shepshalovitch, Jeanne ^a   Hirschberg, Koret ^a  

^a TEL AVIV UNIVERSITY   (Israel)

Author keywords

Endoplasmic reticulum; ER exit sites; Golgi complex; Live cell imaging; Secretory transport; Transmembrane domain

Indexed keywords

GOLGI RESIDENT PROTEIN GALT; MEMBRANE PROTEIN; MUTANT PROTEIN; UNCLASSIFIED DRUG; VESICULAR STOMATITIS VIRUS G TSO45;

ALPHA HELIX; AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DELETION MUTANT; ENDOPLASMIC RETICULUM; GENE INSERTION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN SECRETION; PROTEIN TARGETING; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; TEMPERATURE SENSITIVITY;

AMINO ACID SEQUENCE; ANIMALS; CERCOPITHECUS AETHIOPS; COS CELLS; GALACTOSYLTRANSFERASES; MEMBRANE GLYCOPROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; VIRAL ENVELOPE PROTEINS;

VESICULAR STOMATITIS VIRUS;

EID: 69449102282     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.039339     Document Type: Article

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