Structural determinants in GABARAP required for the selective binding and recruitment of ALFY to LC3B-positive structures.
EMBO Rep
; 15(5): 557-65, 2014 May.
Article
en En
| MEDLINE
| ID: mdl-24668264
ABSTRACT
Several autophagy proteins contain an LC3-interacting region (LIR) responsible for their interaction with Atg8 homolog proteins. Here, we show that ALFY binds selectively to LC3C and the GABARAPs through a LIR in its WD40 domain. Binding of ALFY to GABARAP is indispensable for its recruitment to LC3B-positive structures and, thus, for the clearance of certain p62 structures by autophagy. In addition, the crystal structure of the GABARAP-ALFY-LIR peptide complex identifies three conserved residues in the GABARAPs that are responsible for binding to ALFY. Interestingly, introduction of these residues in LC3B is sufficient to enable its interaction with ALFY, indicating that residues outside the LIR-binding hydrophobic pockets confer specificity to the interactions with Atg8 homolog proteins.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Autofagia
/
Factores de Transcripción
/
Proteínas Adaptadoras Transductoras de Señales
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Proteínas de la Membrana
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Proteínas Asociadas a Microtúbulos
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
EMBO Rep
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2014
Tipo del documento:
Article
País de afiliación:
Noruega