A transmembrane segment determines the steady-state localization of ion-transporting adenosine triphosphatase

Journal of Cell Biology

Volumn 148, Issue 4, 2000, Pages 769-778

  Dunbar, Lisa A ^a   Aronson, Paul ^a   Caplan, Michael J ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Epithelia; H,K ATPase; Na,K ATPase; Polarity; Sorting

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); GLYCOSPHINGOLIPID; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE;

ACID SECRETION; ANIMAL CELL; ARTICLE; CELL COMPARTMENTALIZATION; CELL POLARITY; CELL SELECTION; CHIMERA; ENZYME LOCALIZATION; ENZYME SUBUNIT; GENETIC TRANSFECTION; ION TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; RAT; STOMACH PARIETAL CELL;

AMINO ACID SEQUENCE; ANIMALS; BIOLOGICAL TRANSPORT; CATIONS; CELL LINE; CELL MEMBRANE; CELL POLARITY; GLYCOSPHINGOLIPIDS; GLYCOSYLPHOSPHATIDYLINOSITOLS; H(+)-K(+)-EXCHANGING ATPASE; HYDROGEN-ION CONCENTRATION; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; NA(+)-K(+)-EXCHANGING ATPASE; OUABAIN; PARIETAL CELLS, GASTRIC; PROTEIN SORTING SIGNALS; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE DELETION; SOLUBILITY; TRANSFECTION;

EID: 0034695917     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.148.4.769     Document Type: Article

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