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Titolo:
SPECIFIC BINDING OF ACIDIC PHOSPHOLIPIDS TO MICROTUBULE-ASSOCIATED PROTEIN MAP1B REGULATES ITS INTERACTION WITH TUBULIN
Autore:
YAMAUCHI E; TITANI K; TANIGUCHI H;
Indirizzi:
FUJITA HLTH UNIV,SCH MED,INST COMPREHENS MED SCI,DEPT BIOMED POLYMER SCI TOYOAKE AICHI 47011 JAPAN FUJITA HLTH UNIV,SCH MED,INST COMPREHENS MED SCI,DEPT BIOMED POLYMER SCI TOYOAKE AICHI 47011 JAPAN NAGOYA CITY UNIV,FAC PHARMACEUT SCI,DEPT BIOL CHEM,MIZUHO KU NAGOYA AICHI 467 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 36, volume: 272, anno: 1997,
pagine: 22948 - 22953
SICI:
0021-9258(1997)272:36<22948:SBOAPT>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
KINASE-C SUBSTRATE; ALZHEIMERS-DISEASE; RAT-BRAIN; MEMBRANE PHOSPHOLIPIDS; MESSENGER-RNA; PHOSPHORYLATION; TAU; IDENTIFICATION; DOMAIN; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
E. Yamauchi et al., "SPECIFIC BINDING OF ACIDIC PHOSPHOLIPIDS TO MICROTUBULE-ASSOCIATED PROTEIN MAP1B REGULATES ITS INTERACTION WITH TUBULIN", The Journal of biological chemistry, 272(36), 1997, pp. 22948-22953

Abstract

Microtubule-associated protein MAP1B, a major neuronal cytoskeletal protein, is expressed highly during the early stage of brain development and is thought to play an important role in brain development. Although it has been shown that MAP1B localizes both in cytosol and particulate fractions, the underlying molecular mechanism in the membrane localization has yet to be elucidated. In the present study, we show thatMAP1B purified from young rat brain can bind to acidic phospholipids,such as phosphatidylserine, but not to a neutral phospholipid, phosphatidylcholine. Furthermore, the binding of MAP1B to taxol-stabilized microtubules was inhibited by the addition of phosphatidylserine or phosphatidylinositol. The addition of phosphatidylcholine showed no effect on the binding of MAP1B to the microtubules. A 120-kDa microtubule-binding fragment of MAP1B was also released from microtubules by the addition of acidic phospholipids. Synthetic peptides derived from the C-terminal half of the tubulin-binding domain, but not that corresponding to the N-terminal half, bound to acidic phospholipids specifically. These results suggest that MAP1B binds to biological membranes throughits tubulin-binding site, and the binding may play a regulatory role in MAP1B-microtubule interaction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 19:47:59