Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of alpha-actinin.
BMC Cell Biol
; 10: 22, 2009 Mar 27.
Article
em En
| MEDLINE
| ID: mdl-19327143
ABSTRACT
BACKGROUND:
The PDZ-LIM proteins are a family of signalling adaptors that interact with the actin cross-linking protein, alpha-actinin, via their PDZ domains or via internal regions between the PDZ and LIM domains. Three of the PDZ-LIM proteins have a conserved 26-residue ZM motif in the internal region, but the structure of the internal region is unknown.RESULTS:
In this study, using circular dichroism and nuclear magnetic resonance (NMR), we showed that the ALP internal region (residues 107-273) was largely unfolded in solution, but was able to interact with the alpha-actinin rod domain in vitro, and to co-localize with alpha-actinin on stress fibres in vivo. NMR analysis revealed that the titration of ALP with the alpha-actinin rod domain induces stabilization of ALP. A synthetic peptide (residues 175-196) that contained the N-terminal half of the ZM motif was found to interact directly with the alpha-actinin rod domain in surface plasmon resonance (SPR) measurements. Short deletions at or before the ZM motif abrogated the localization of ALP to actin stress fibres.CONCLUSION:
The internal region of ALP appeared to be largely unstructured but functional. The ZM motif defined part of the interaction surface between ALP and the alpha-actinin rod domain.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Actinina
/
Proteínas dos Microfilamentos
Tipo de estudo:
Risk_factors_studies
Limite:
Humans
Idioma:
En
Revista:
BMC Cell Biol
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Finlândia