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Titolo:
THE ROD DOMAIN OF NF-L DETERMINES NEUROFILAMENT ARCHITECTURE, WHEREASTHE END DOMAINS SPECIFY FILAMENT ASSEMBLY AND NETWORK FORMATION
Autore:
HEINS S; WONG PC; MULLER S; GOLDIE K; CLEVELAND DW; AEBI U;
Indirizzi:
UNIV BASEL,BIOCTR,ME MULLER INST,KLINGELBERGSTR 70 CH-4056 BASEL SWITZERLAND UNIV BASEL,BIOCTR,ME MULLER INST,KLINGELBERGSTR 70 CH-4056 BASEL SWITZERLAND JOHNS HOPKINS UNIV,SCH MED,DEPT BIOL CHEM BALTIMORE MD 21205 JOHNS HOPKINS UNIV,SCH MED,DEPT NEUROSCI BALTIMORE MD 21205 JOHNS HOPKINS UNIV,SCH MED,DEPT CELL BIOL & ANAT BALTIMORE MD 21205
Titolo Testata:
The Journal of cell biology
fascicolo: 6, volume: 123, anno: 1993,
parte:, 1
pagine: 1517 - 1533
SICI:
0021-9525(1993)123:6<1517:TRDOND>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN EPIDERMAL KERATIN; 1/KERATIN-10 INTERMEDIATE FILAMENTS; EPIDERMOLYSIS-BULLOSA SIMPLEX; TERMINALLY DELETED DESMIN; COILED-COIL MOLECULES; VIMENTIN HEAD DOMAIN; AMINO-ACID-SEQUENCE; LAMIN-A; SYNTHETIC PEPTIDES; PROTOFILAMENT UNIT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
93
Recensione:
Indirizzi per estratti:
Citazione:
S. Heins et al., "THE ROD DOMAIN OF NF-L DETERMINES NEUROFILAMENT ARCHITECTURE, WHEREASTHE END DOMAINS SPECIFY FILAMENT ASSEMBLY AND NETWORK FORMATION", The Journal of cell biology, 123(6), 1993, pp. 1517-1533

Abstract

Neurofilaments, assembled from NF-L, NF-M, and NF-H subunits, are themost abundant structural elements in myelinated axons. Although all three subunits contain a central, alpha-helical rod domain thought to mediate filament assembly, only NF-L self-assembles into 10-nm filaments in vitro. To explore the roles of the central rod, the NH2-terminal head and the COOH-terminal tail domain in filament assembly, full-length, headless, tailless, and rod only fragments of mouse NF-L were expressed in bacteria, purified, and their structure and assembly properties examined by conventional and scanning transmission electron microscopy (TEM and STEM). These experiments revealed that in vitro assembly of NF-L into bona fide 10-nm filaments requires both end domains: whereas the NH2-terminal head domain promotes lateral association of protofilaments into protofibrils and ultimately 10-nm filaments, the COOH-terminal tail domain controls lateral assembly of protofilaments so that it terminates at the 10-nm filament level. Hence, the two end domains of NF-L have antagonistic effects on the lateral association of protofilaments into higher-order structures, with the effect of the COOH-terminal tail domain being dominant over that of the NH2-terminal head domain. Consideration of the 21-nm axial beading commonly observed with 10-nm filaments, the approximate 21-nm axial periodicity measured onparacrystals, and recent cross-linking data combine to support a molecular model for intermediate filament architecture in which the 44-46-nm long dimer rods overlap by 1-3-nm head-to-tail, whereas laterally they align antiparallel both unstaggered and approximately half-staggered.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 00:10:25