Down-regulation of protein-tyrosine phosphatases activates an immune receptor in the absence of its translocation into lipid rafts

Journal of Biological Chemistry

Volumn 285, Issue 17, 2010, Pages 12787-12802

  Heneberg, Petr ^a   Dráberová, Lubica ^a   Bambousková, Monika ^a   Pompach, Petr ^b   Dráber, Petr ^a  

^a INSTITUTE OF MOLECULAR GENETICS   (Czech Republic)

^b INSTITUTE OF MICROBIOLOGY   (Czech Republic)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN CYTOSKELETON; ACTIVE SITE; BONE MARROW-DERIVED MAST CELLS; DETERGENT-RESISTANT MEMBRANES; DOWN-REGULATION; ENZYMATIC ACTIVITIES; HIGH AFFINITY; IMMUNE RECEPTORS; IMMUNE RECOGNITION; IN-CELL; LEUKEMIA CELLS; LIGAND BINDING; LIPID RAFT; MAST CELLS; MOLECULAR MECHANISM; OXIDATION STATE; PLASMA MEMBRANES; PROTEIN-TYROSINE PHOSPHATASE; SHARP CONTRAST; SRC-FAMILY KINASE; TYROSINE PHOSPHORYLATION;

AMINO ACIDS; ANTIGENS; CELL MEMBRANES; OXIDATION; PHOSPHORYLATION; PROTEINS; SCANNING ELECTRON MICROSCOPY;

PHOSPHATASES;

ACTIN; ANTIGEN; CYSTEINE; HYDROGEN PEROXIDE; IMMUNOGLOBULIN E RECEPTOR; PERVANADATE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEIN TYROSINE PHOSPHATASE SHP 2;

ANIMAL CELL; ARTICLE; CELL LINE; CELL MEMBRANE; CONTROLLED STUDY; CYTOSKELETON; DOWN REGULATION; ELECTRON MICROSCOPY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME LOCALIZATION; ENZYME METABOLISM; ENZYME SUBSTRATE; GENE TRANSLOCATION; LEUKEMIA CELL; LIPID RAFT; MAST CELL; MOLECULAR MECHANICS; MOUSE; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; RAT;

ANIMALS; ANTIGENS; CELL LINE, TUMOR; ENZYME ACTIVATION; ENZYME INHIBITORS; HYDROGEN PEROXIDE; MAST CELLS; MEMBRANE MICRODOMAINS; MICE; OXIDANTS; OXIDATION-REDUCTION; PHOSPHORYLATION; PROTEIN TRANSPORT; PROTEIN TYROSINE PHOSPHATASES; RATS; RECEPTORS, IGE; SRC-FAMILY KINASES; VANADATES;

RATTUS;

EID: 77951224086     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.052555     Document Type: Article

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