http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17427
Concerted mutation of Phe residues belonging to the beta-dystroglycan ectodomain strongly inhibits the interaction with alpha-dystroglycan in vitro (Articolo in rivista)
- Type
- Label
- Concerted mutation of Phe residues belonging to the beta-dystroglycan ectodomain strongly inhibits the interaction with alpha-dystroglycan in vitro (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Alternative label
Bozzi M., Sciandra F., Ferri L., Torreri P., Pavoni E., Petrucci T.C., Giardina B., Brancaccio A. (2006)
Concerted mutation of Phe residues belonging to the beta-dystroglycan ectodomain strongly inhibits the interaction with alpha-dystroglycan in vitro
in The FEBS journal (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Bozzi M., Sciandra F., Ferri L., Torreri P., Pavoni E., Petrucci T.C., Giardina B., Brancaccio A. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- PubMe (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Bozzi M.: Istituto di Biochimica e Biochimica Clinica, UCSC
Torreri P.; Petrucci T.C.: Dipartimento di Biologia Cellulare e Neuroscienze, Istituto Superiore di Sanita`
Sciandra F., Ferri L., Pavoni E., Giardina B., Brancaccio A.: CNR, Istituto di Chimica del Riconoscimento Molecolare (literal)
- Titolo
- Concerted mutation of Phe residues belonging to the beta-dystroglycan ectodomain strongly inhibits the interaction with alpha-dystroglycan in vitro (literal)
- Abstract
- The dystroglycan adhesion complex consists of two noncovalently interacting
proteins: alpha-dystroglycan, a peripheral extracellular subunit that is
extensively glycosylated, and the transmembrane beta-dystroglycan, whose
cytosolic tail interacts with dystrophin, thus linking the F-actin cytoskeleton
to the extracellular matrix. Dystroglycan is thought to play a crucial
role in the stability of the plasmalemma, and forms strong contacts
between the extracellular matrix and the cytoskeleton in a wide variety of
tissues. Abnormal membrane targeting of dystroglycan subunits and ? or
their aberrant post-translational modification are often associated with
several pathologic conditions, ranging from neuromuscular disorders to
carcinomas. A putative functional hotspot of dystroglycan is represented
by its intersubunit surface, which is contributed by two amino acid stretches:
approximately 30 amino acids of b-dystroglycan (691-719), and
approximately 15 amino acids of a-dystroglycan (550-565). Exploiting
alanine scanning, we have produced a panel of site-directed mutants of
our two consolidated recombinant peptides beta-dystroglycan (654-750),
corresponding to the ectodomain of beta-dystroglycan, and alpha-dystroglycan
(485-630), spanning the C-terminal domain of alpha-dystroglycan. By solid-phase
binding assays and surface plasmon resonance, we have determined
the binding affinities of mutated peptides in comparison to those of wildtype
alpha-dystroglycan and beta-dystroglycan, and shown the crucial role of two
beta-dystroglycan phenylalanines, namely Phe692 and Phe718, for the alpha-beta
interaction. Substitution of the a-dystroglycan residues Trp551, Phe554
and Asn555 by Ala does not affect the interaction between dystroglycan
subunits in vitro. As a preliminary analysis of the possible effects of the
aforementioned mutations in vivo, detection through immunofluorescence
and western blot of the two dystroglycan subunits was pursued in dystroglycan-
transfected 293-Ebna cells. (literal)
- Prodotto di
- Autore CNR
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi