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Titolo:
INTERMEDIATE FILAMENT DISASSEMBLY IN CULTURED DORSAL-ROOT GANGLION NEURONS IS ASSOCIATED WITH AMINO-TERMINAL HEAD DOMAIN PHOSPHORYLATION OFSPECIFIC SUBUNITS
Autore:
GIASSON BI; MUSHYNSKI WE;
Indirizzi:
MCGILL UNIV,DEPT BIOCHEM,3655 DRUMMOND ST,ROOM 802 MONTREAL PQ H3G 1Y6 CANADA MCGILL UNIV,DEPT BIOCHEM MONTREAL PQ H3G 1Y6 CANADA
Titolo Testata:
Journal of neurochemistry
fascicolo: 5, volume: 70, anno: 1998,
pagine: 1869 - 1875
SICI:
0022-3042(1998)70:5<1869:IFDICD>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT PROTEIN-KINASE; ACID-TREATED NEURONS; NEUROFILAMENT SUBUNIT; NF-L; DYNAMICS; IDENTIFICATION; PHOSPHATASES; PERIPHERIN; INVITRO; SITE;
Keywords:
ASSEMBLY; ALPHA-INTERNEXIN; NEUROFILAMENT; PERIPHERIN; PHOSPHATASE; PROTEIN KINASE A;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
B.I. Giasson e W.E. Mushynski, "INTERMEDIATE FILAMENT DISASSEMBLY IN CULTURED DORSAL-ROOT GANGLION NEURONS IS ASSOCIATED WITH AMINO-TERMINAL HEAD DOMAIN PHOSPHORYLATION OFSPECIFIC SUBUNITS", Journal of neurochemistry, 70(5), 1998, pp. 1869-1875

Abstract

We previously reported that activation of protein kinase A in cultured rat dorsal root ganglion neurons, treated concomitantly with low concentrations of okadaic acid that selectively inhibit protein phosphatase-2A, enhanced the Triton X-100 solubility of neurofilament triplet proteins. We now show that peripherin and alpha-internexin follow the same fragmentation profile as the neurofilament subunits, consistent with the notion that all five cytoplasmic intermediate filament proteinsin these neurons form an integrated filamentous network whose assembly can be modulated by protein kinase A. Similar to the situation previously observed for the light neurofilament subunit, there was a strongcorrelation between phosphorylation of the amino-terminal head domainof peripherin and filament fragmentation. In contrast, insignificant levels of P-32 were incorporated into alpha-internexin under conditions promoting disassembly, indicating that phosphorylation of this protein is not involved directly in filament fragmentation. The situation for the mid-sized neurofilament subunit (NFM) was not as clear-cut. Phosphopeptide mapping of NFM revealed many head and tail domain phosphorylation sites. However, changes in NFM head domain phosphorylation under conditions promoting filament disassembly were not as pronounced asfor peripherin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/08/20 alle ore 23:15:13