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Titolo:
MOLECULAR-STRUCTURE OF THE SARCOMERIC Z-DISK - 2 TYPES OF TITIN INTERACTIONS LEAD TO AN ASYMMETRICAL SORTING OF ALPHA-ACTININ
Autore:
YOUNG P; FERGUSON C; BANUELOS S; GAUTEL M;
Indirizzi:
EUROPEAN MOL BIOL LAB,POSTFACH 102209 D-69012 HEIDELBERG GERMANY EUROPEAN MOL BIOL LAB D-69012 HEIDELBERG GERMANY
Titolo Testata:
EMBO journal
fascicolo: 6, volume: 17, anno: 1998,
pagine: 1614 - 1624
SICI:
0261-4189(1998)17:6<1614:MOTSZ->2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
Z-BAND; 3-DIMENSIONAL STRUCTURE; SKELETAL-MUSCLE; F-ACTIN; PROTEINS; SPECTRIN; REGION; LINE; MYOFIBRILLOGENESIS; ULTRASTRUCTURE;
Keywords:
ALPHA-ACTININ; CONNECTIN; MUSCLE STRUCTURE; NEBULIN; TITIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
P. Young et al., "MOLECULAR-STRUCTURE OF THE SARCOMERIC Z-DISK - 2 TYPES OF TITIN INTERACTIONS LEAD TO AN ASYMMETRICAL SORTING OF ALPHA-ACTININ", EMBO journal, 17(6), 1998, pp. 1614-1624

Abstract

The sarcomeric Z-disk, the anchoring plane of thin (actin) filaments,links titin (also called connectin) and actin filaments from opposingsarcomere halves in a lattice connected by alpha-actinin. We demonstrate by protein interaction analysis that two types of titin interactions are involved in the assembly of alpha-actinin into the Z-disk. Titin interacts via a single binding site with the two central spectrin-like repeats of the outermost pair of alpha-actinin molecules. In the central Z-disk, titin can interact with multiple alpha-actinin moleculesvia their C-terminal domains. These interactions allow the assembly of a ternary complex of titin, actin and alpha-actinin in vitro, and are expected to constrain the path of titin in the Z-disk. In thick skeletal muscle Z-disks, titin filaments cross over the Z-disk centre by similar to 30 nn, suggesting that their alpha-actinin-binding sites overlap in an antiparallel fashion. The combination of our biochemical and ultrastructural data now allows a molecular model of the sarcomeric Z-disk, where overlapping titin filaments and their interactions with the alpha-actinin rod and C-terminal domain can account for the essential ultrastructural features.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 21:51:58