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Titolo:
The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism
Autore:
Young, P; Gautel, M;
Indirizzi:
Max Planck Inst Mol Physiol, Phys Biochem Abt, D-44202 Dortmund, Germany Max Planck Inst Mol Physiol Dortmund Germany D-44202 2 Dortmund, Germany European Mol Biol Lab, Struct Biol Div, D-69012 Heidelberg, Germany European Mol Biol Lab Heidelberg Germany D-69012 012 Heidelberg, Germany
Titolo Testata:
EMBO JOURNAL
fascicolo: 23, volume: 19, anno: 2000,
pagine: 6331 - 6340
SICI:
0261-4189(200012)19:23<6331:TIOTAA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
Z-DISK; MUSCLE DIFFERENTIATION; FOCAL ADHESIONS; SKELETAL-MUSCLE; CAPPING PROTEIN; STRESS FIBERS; REPEAT MOTIFS; LIM PROTEIN; Z-BAND; BINDING;
Keywords:
alpha-actinin; connectin; phosphatidylinositides; phosphatidylinositide kinases; titin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
66
Recensione:
Indirizzi per estratti:
Indirizzo: Gautel, M Max Planck Inst Mol Physiol, Phys Biochem Abt, Postfach 500 247,D-44202 Dortmund, Germany Max Planck Inst Mol Physiol Postfach 500 247 Dortmund Germany D-44202
Citazione:
P. Young e M. Gautel, "The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism", EMBO J, 19(23), 2000, pp. 6331-6340

Abstract

The assembly of stable cytoskeletal structures from dynamically recycled molecules requires developmental and spatial regulation of protein interactions. In muscle, titin acts as a molecular ruler organizing the actin cytoskeleton via interactions with many sarcomeric proteins, including the crosslinking protein alpha -actinin. An interaction between the C-terminal domainof alpha -actinin and titin Z-repeat motifs targets alpha -actinin to the Z-disk. Here we investigate the cellular regulation of this interaction. alpha -actinin is a rod shaped head-to-tail homodimer. In contrast to C-terminal fragments, full-length alpha -actinin does not bind Z-repeats. We identify a 30-residue Z-repeat homologous sequence between the actin-binding androd regions of alpha -actinin that binds the C-terminal domain with nanomolar affinity. Thus, Z-repeat binding is prevented by this 'pseudoligand' interaction between the subunits of the alpha -actinin dimer. This autoinhibition is relieved upon binding of the Z-disk lipid phosphatidylinositol-bisphosphate to the actin-binding domain. We suggest that this novel mechanism is relevant to control the site-specific interactions of alpha -actinin during sarcomere assembly and turnover. The intramolecular contacts defined here also constrain a structural model for intrasterical regulation of all alpha -actinin isoforms.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 15:16:34