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Titolo:
Microtubule/MAP-affinity regulating kinase (MARK) is activated by phenylarsine oxide in situ and phosphorylates tau within its microtubule-binding domain
Autore:
Jenkins, SM; Johnson, GVW;
Indirizzi:
Univ Alabama, Dept Psychiat, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 t Psychiat, Birmingham, AL 35294 USA
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 4, volume: 74, anno: 2000,
pagine: 1463 - 1468
SICI:
0022-3042(200004)74:4<1463:MRK(IA>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE; P110(MARK); SER(262); BRAIN; MAP2;
Keywords:
microtubule-associated protein; tau; phosphorylation; microtubule/MAP-affinity regulating kinase; phenylarsine oxide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Johnson, GVW Univ Alabama, Dept Psychiat, 1720 7th Ave S,Sparks Ctr,Room 1061, Birmingham, AL 35294 USA Univ Alabama 1720 7th Ave S,Sparks Ctr,Room 1061 Birmingham AL USA 35294
Citazione:
S.M. Jenkins e G.V.W. Johnson, "Microtubule/MAP-affinity regulating kinase (MARK) is activated by phenylarsine oxide in situ and phosphorylates tau within its microtubule-binding domain", J NEUROCHEM, 74(4), 2000, pp. 1463-1468

Abstract

Tau is a microtubule-associated protein (MAP) that is functionally modulated by phosphorylation and that is hyperphosphorylated in several neurodegenerative diseases. Because phosphorylation regulates both normal and pathological tau functioning, it is of interest to identify the signaling pathwaysand enzymes capable of modulating tau phosphorylation in vivo. Previously,it was demonstrated that in SH-SY5Y human neuroblastoma cells and rat primary cortical cultures tau is phosphorylated at Ser(262/356), within its microtubule-binding domain, by a staurosporine-sensitive protein kinase in response to the vicinal thiol-directed agent phenylarsine oxide, The current study demonstrates the presence of a 100-kDa protein kinase activity in SH-SY5Y cells that associates with microtubules, phosphorylates tau at Ser(262/356), is activated by phenylarsine oxide, and is inhibited by the protein kinase inhibitor staurosporine. Isolation of individual protein bands from apolyacrylamide gel revealed two closely spaced proteins containing Ser(262/356)-directed protein kinase activity. Mass spectrometry analysis indicated that these protein bands correspond to the 100-kDa microtubule/MAP-affinity regulating kinase (MARK), which has been shown previously to phosphorylate tau within its microtubule-binding domain. Immunoblot analysis of the protein kinase bands confirmed this finding, providing the first demonstration that activation of endogenous MARK results in increased tau phosphorylation within its microtubule-binding domain in situ.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 08:45:59