CD98 modulates integrin β1 function in polarized epithelial cells

Journal of Cell Science

Volumn 118, Issue 5, 2005, Pages 889-899

  Cai, Songmin ^a   Bulus, Nada ^a   Fonseca Siesser, Priscilla M ^a   Chen, Dong ^a   Hanks, Steven K ^a   Pozzi, Ambra ^a,b,c   Zent, Roy ^a,b,c  

^a VANDERBILT UNIVERSITY   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

4F2; Adhesion; CD98; Epithelial cell; Integrin 1; Migration

Indexed keywords

BETA1 INTEGRIN; CD98 ANTIGEN; LIGAND; MEMBRANE PROTEIN; MUTANT PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; SCAFFOLD PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID TRANSPORT; ANIMAL CELL; ARTICLE; BASOLATERAL MEMBRANE; BRANCHING MORPHOGENESIS; CELL ADHESION; CELL FUNCTION; CELL MIGRATION; CELL POLARITY; ENZYME INHIBITION; EPITHELIUM CELL; FOCAL ADHESION; GENE OVEREXPRESSION; GENE SEQUENCE; HEAVY CHAIN; HUMAN; HUMAN CELL; KIDNEY EPITHELIUM; LIGAND BINDING; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; ORTHOLOGY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RECEPTOR AFFINITY; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION;

1-PHOSPHATIDYLINOSITOL 3-KINASE; AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, CD; ANTIGENS, CD29; ANTIGENS, CD98; ANTIGENS, DIFFERENTIATION, T-LYMPHOCYTE; CELL ADHESION; CELL MEMBRANE; CELL MOVEMENT; COLLAGEN; CYTOPLASM; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; EPITHELIAL CELLS; FOCAL ADHESION KINASE 1; FOCAL ADHESION PROTEIN-TYROSINE KINASES; HUMANS; IMMUNOBLOTTING; IMMUNOPRECIPITATION; INTEGRINS; KIDNEY; LIGANDS; MICE; MICROSCOPY, FLUORESCENCE; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-AKT; SEQUENCE HOMOLOGY, AMINO ACID;

ANIMALIA;

EID: 16844376662     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01674     Document Type: Article

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