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Titolo:
Alternative splicing of dystrobrevin regulates the stoichiometry of syntrophin binding to the dystrophin protein complex
Autore:
Newey, SE; Benson, MA; Ponting, CP; Davies, KE; Blake, DJ;
Indirizzi:
Univ Oxford, Dept Human Anat & Genet, Oxford OX1 3QX, England Univ OxfordOxford England OX1 3QX Anat & Genet, Oxford OX1 3QX, England MRC, Funct Genet Unit, Dept Human Anat & Genet, Oxford OX1 3QX, England MRC Oxford England OX1 3QX t Human Anat & Genet, Oxford OX1 3QX, England
Titolo Testata:
CURRENT BIOLOGY
fascicolo: 20, volume: 10, anno: 2000,
pagine: 1295 - 1298
SICI:
0960-9822(20001019)10:20<1295:ASODRT>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUSCULAR-DYSTROPHIES; ALPHA-DYSTROBREVIN; BETA-DYSTROBREVIN; SKELETAL-MUSCLE; FAMILY; ALPHA-1-SYNTROPHIN; BETA-2-SYNTROPHIN; IDENTIFICATION; TERMINUS; DOMAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Davies, KE Univ Oxford, Dept Human Anat & Genet, S Parks Rd, Oxford OX1 3QX, England Univ Oxford S Parks Rd Oxford England OX1 3QX OX1 3QX, England
Citazione:
S.E. Newey et al., "Alternative splicing of dystrobrevin regulates the stoichiometry of syntrophin binding to the dystrophin protein complex", CURR BIOL, 10(20), 2000, pp. 1295-1298

Abstract

Dystrophin coordinates the assembly of a complex of structural and signalling proteins that is required for normal muscle function, A key component of the dystrophin-associated protein complex (DPC) is alpha -dystrobrevin, adystrophin-related and -associated protein whose absence results in muscular dystrophy and neuromuscular junction defects [1,2]. The current model ofthe DPC predicts that dystrophin and dystrobrevin each bind a single syntrophin molecule [3], The syntrophins are PDZ-domain-containing proteins thatfacilitate the recruitment of signalling proteins such as nNOS (neuronal nitric oxide synthase) to the DPC [4], Here we show, using yeast two-hybrid analysis and biochemical binding studies, that alpha -dystrobrevin in fact contains two independent syntrophin-binding sites in tandem. The previouslyundescribed binding site is situated within an alternatively spliced exon of alpha -dystrobrevin, termed the variable region-3 (vr3) sequence, which is specifically expressed in skeletal and cardiac muscle [5,6]. Analysis ofthe syntrophin-binding region of dystrobrevin reveals a tandem pair of predicted a helices with significant sequence similarity. These a helices, each termed a syntrophin-binding motif, are also highly conserved in dystrophin and utrophin, Together these data show that there are four potential syntrophin-binding sites per dystrophin complex in skeletal muscle: two on dystrobrevin and two on dystrophin or utrophin, Furthermore, alternative splicing of dystrobrevin provides a mechanism for regulating the stoichiometry ofsyntrophin association with the DPc, This is likely to have important consequences for the recruitment of specific signalling molecules to the DPc and ultimately for its function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 09:58:03