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Titolo:
FE65 AND THE PROTEIN NETWORK CENTERED AROUND THE CYTOSOLIC DOMAIN OF THE ALZHEIMERS BETA-AMYLOID PRECURSOR PROTEIN
Autore:
RUSSO T; FARAONIO R; MINOPOLI G; DECANDIA P; DERENZIS S; ZAMBRANO N;
Indirizzi:
UNIV NAPLES FEDERICO II,DIPARTIMENTO BIOCHIM & BIOTECNOL MED,VIA S PANSINI 5 I-80131 NAPLES ITALY
Titolo Testata:
FEBS letters
fascicolo: 1-2, volume: 434, anno: 1998,
pagine: 1 - 7
SICI:
0014-5793(1998)434:1-2<1:FATPNC>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOTYROSINE-BINDING DOMAIN; DNA-BINDING; CYTOPLASMIC DOMAIN; SECRETASE CLEAVAGE; CORTICAL-NEURONS; WW DOMAIN; DISEASE; GENE; CELLS; SHC;
Keywords:
FE65; BETA-AMYLOID PRECURSOR PROTEIN; PROTEIN-PROTEIN INTERACTION; ALZHEIMER; AMYLOID;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
T. Russo et al., "FE65 AND THE PROTEIN NETWORK CENTERED AROUND THE CYTOSOLIC DOMAIN OF THE ALZHEIMERS BETA-AMYLOID PRECURSOR PROTEIN", FEBS letters, 434(1-2), 1998, pp. 1-7

Abstract

A distinctive tract of all the forms of Alzheimer's disease is the extracellular deposition of a 40-42/43 amino acid-long peptide derived from the so-called beta-amyloid precursor protein (APP), This is a membrane protein of unknown function, whose short cytosolic domain has been recently demonstrated to interact with several proteins. One of these proteins, named Fe65, has the characteristics of an adaptor protein;in fact, it possesses three protein-protein interaction domains: a WWdomain and two PID/PTB domains. The interaction with APP requires themost C-terminal PID/PTB domain, whereas the WW domain is responsible for the interaction with various proteins, one of which was demonstrated to be the mammalian homolog of the Drosophila enabled protein (Mena), which in turn interacts with the cytoskeleton, The second PID/PTB domain of Fe65 binds to the CP2/LSF/LBP1 protein, which is an already known transcription factor. The other proteins interacting with the cytosolic domain of APP are the G(o) heterotrimeric protein, APP-BP1 and X11, The latter interacts with APP through a PID/PTB domain and possesses two other protein-protein interaction domains. The small size of the APP cytodomain and the overlapping of its regions involved in the binding of Fe65 and X11 suggest the existence of competitive mechanismsregulating the binding of the various ligands to this cytosolic domain. In this short review the possible functional roles of this complex protein network and its involvement in the generation of Alzheimer's phenotype are discussed. (C) 1998 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 09:27:30