Peptide EphB2/CTF2 generated by the γ-secretase processing of EphB2 receptor promotes tyrosine phosphorylation and cell surface localization of N-methyl-D-aspartate receptors

Journal of Biological Chemistry

Volumn 284, Issue 40, 2009, Pages 27220-27228

  Xu, Jindong ^a   Litterst, Claudia ^a,b   Georgakopoulos, Anastasios ^a   Zaganas, Ioannis ^a,c   Robakis, Nikolaos K ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^b BIO RAD LABORATORIES   (United States)

^c UNIVERSITY HOSPITAL OF HERAKLION   (Greece)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; CELL LINES; CELL SURFACE EXPRESSION; CELL SURFACE PROTEINS; CELL SURFACE RECEPTORS; CELL SURFACES; CYTOSOLIC; CYTOSOLS; FUNCTIONAL COMPONENTS; LEARNING AND MEMORY; N METHYL D ASPARTATE RECEPTOR; N-METHYL-D-ASPARTATE; PRESENILINS; PROTEIN PHOSPHORYLATION; SECRETASE COMPLEX; SECRETASES; SRC-KINASE; SYNAPTIC PLASTICITY; TYROSINE KINASE; TYROSINE PHOSPHORYLATION;

AMINES; AMINO ACIDS; CELL CULTURE; PEPTIDES; PHOSPHORYLATION; SIGNAL TRANSDUCTION;

CELL MEMBRANES;

EPHRIN RECEPTOR B2; GAMMA SECRETASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PRESENILIN 1; PROTEIN TYROSINE KINASE; PEPTIDE FRAGMENT; PROTEIN SUBUNIT; SECRETASE; TYROSINE;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CELL LINE; CELL SURFACE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOSOL; EMBRYO; ENZYME ACTIVITY; LEARNING; MEMORY; NERVE CELL; NERVE CELL PLASTICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; RAT; WISTAR RAT; ANIMAL; CHEMISTRY; CYTOLOGY; GENE EXPRESSION REGULATION; HUMAN; METABOLISM; MOUSE; PHOSPHORYLATION; PROTEIN TRANSPORT;

AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; CELL LINE; CYTOSOL; GENE EXPRESSION REGULATION; HUMANS; MICE; NEURONS; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN SUBUNITS; PROTEIN TRANSPORT; PROTEIN-TYROSINE KINASES; RATS; RATS, WISTAR; RECEPTOR, EPHB2; RECEPTORS, N-METHYL-D-ASPARTATE; TYROSINE;

EID: 70350444721     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.048728     Document Type: Article

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