Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PERIPHERIN IS TYROSINE-PHOSPHORYLATED AT ITS CARBOXYL-TERMINAL TYROSINE
Autore:
ANGELASTRO JM; HO CL; FRAPPIER T; LIEM RKH; GREENE LA;
Indirizzi:
COLUMBIA UNIV COLL PHYS & SURG,DEPT PATHOL,630 W 168TH ST NEW YORK NY10032 COLUMBIA UNIV COLL PHYS & SURG,CTR NEUROBIOL & BEHAV NEW YORK NY 10032
Titolo Testata:
Journal of neurochemistry
fascicolo: 2, volume: 70, anno: 1998,
pagine: 540 - 549
SICI:
0022-3042(1998)70:2<540:PITAIC>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTERMEDIATE FILAMENT PROTEIN; NERVE GROWTH-FACTOR; HEAD DOMAIN; PC12 CELLS; KINASE-A; EXPRESSION; VIMENTIN; RAT; PHOSPHOTYROSINE; IDENTIFICATION;
Keywords:
INTERMEDIATE FILAMENT; PERIPHERIN; PHOSPHOTYROSINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
J.M. Angelastro et al., "PERIPHERIN IS TYROSINE-PHOSPHORYLATED AT ITS CARBOXYL-TERMINAL TYROSINE", Journal of neurochemistry, 70(2), 1998, pp. 540-549

Abstract

Peripherin is a type III intermediate filament present in peripheral and certain CNS neurons, We report here that peripherin contains a phosphotyrosine residue and, as such, is the only identified intermediatefilament protein known to be modified in this manner. Antiserum specific for phosphotyrosine recognizes peripherin present in PC12 cells (with or without nerve growth factor treatment) and in rat sciatic nerveas well as that expressed in Sf-9 cells and SW-13 cl. 2 vim(-) cells. The identity of peripherin as a tyrosine-phosphorylated protein in PC12 cells was confirmed by immunoprecipitation, two-dimensional isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels, and phosphoamino acid analysis. Unlike serine/threonine phosphorylation, tyrosine phosphorylation of peripherin is not regulated by depolarization or nerve growth factor treatment, To identify the site of tyrosine phosphorylation, rat peripherin was mutated at several tyrosine residues and expressed in SW-13 ct. 2 vim(-) cells. Tyrosine phosphorylation was selectively lost only for peripherin mutants in whichthe carboxy-terminal tyrosine (Y474) was mutated. Indirect immunofluorescence staining indicated that both wild-type peripherin and peripherin Y474F form a filamentous network in SW-13 cl. 2 vim(-) cells. Thisindicates that tyrosine phosphorylation of the peripherin C-terminal residue is not required for assembly and leaves open the possibility that this modification serves other functions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 08:57:45