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Titolo:
Molecular cloning and characterization of phocein, a protein found from the Golgi complex to dendritic spines
Autore:
Baillat, G; Moqrich, A; Castets, F; Baude, AS; Bailly, Y; Benmerah, A; Monneron, A;
Indirizzi:
CNRS, FRE 9041, F-13009 Marseille, France CNRS Marseille France F-13009CNRS, FRE 9041, F-13009 Marseille, France CNRS, FRE 9024, F-13009 Marseille, France CNRS Marseille France F-13009CNRS, FRE 9024, F-13009 Marseille, France CNRS, FRE 2180, F-67084 Strasbourg, France CNRS Strasbourg France F-67084 NRS, FRE 2180, F-67084 Strasbourg, France Fac Necker Enfants Malad, INSERM E9925, F-75730 Paris, France Fac Necker Enfants Malad Paris France F-75730 925, F-75730 Paris, France
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 3, volume: 12, anno: 2001,
pagine: 663 - 673
SICI:
1059-1524(200103)12:3<663:MCACOP>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALMODULIN-BINDING PROTEIN; BREFELDIN-A; NEURONAL POLARITY; HIPPOCAMPAL-NEURONS; STRIATIN; RAT; GENERATION; EXPRESSION; TRANSPORT; BRAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Monneron, A CNRS, FRE 9041, F-13009 Marseille, France CNRS Marseille France F-13009 041, F-13009 Marseille, France
Citazione:
G. Baillat et al., "Molecular cloning and characterization of phocein, a protein found from the Golgi complex to dendritic spines", MOL BIOL CE, 12(3), 2001, pp. 663-673

Abstract

Phocein is a widely expressed, highly conserved intracellular protein of 225 amino acids, the sequence of which has limited homology to the a subunits from clathrin adaptor complexes and contains an additional stretch bearing a putative SH3-binding domain. This sequence is evolutionarily very conserved (80% identity between Drosophila melanogaster and human). Phocein was discovered by a yeast two-hybrid screen using striatin as a bait. Striatin,SG2NA, and zinedin, the three mammalian members of the striatin family, are multimodular, WD-repeat, and calmodulin-binding proteins. The interactionof phocein with striatin, SG2NA, and zinedin was validated in vitro by coimmunoprecipitation and pull-down experiments. Fractionation of brain and HeLa cells showed that phocein is associated with membranes, as well as present in the cytosol where it behaves as a protein complex. The molecular interaction between SG2NA and phocein was confirmed by their in vivo colocalization, as observed in HeLa cells where antibodies directed against either phocein or SG2NA immunostained the Golgi complex. A 2-min brefeldin A treatment of HeLa cells induced the redistribution of both proteins. Immunocytochemical studies of adult rat brain sections showed that phocein reactivity, present in many types of neurons, is strictly somato-dendritic and extends down to spines, just as do striatin and SG2NA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 06:23:21