ALIX is a Lys63-specific polyubiquitin binding protein that functions in retrovirus budding.
Dev Cell
; 23(6): 1247-54, 2012 Dec 11.
Article
em En
| MEDLINE
| ID: mdl-23201121
ABSTRACT
The diversity of ubiquitin (Ub)-dependent signaling is attributed to the ability of this small protein to form different types of covalently linked polyUb chains and to the existence of Ub binding proteins that interpret this molecular syntax. We used affinity capture/mass spectrometry to identify ALIX, a component of the ESCRT pathway, as a Ub binding protein. We report that the V domain of ALIX binds directly and selectively to K63-linked polyUb chains, exhibiting a strong preference for chains composed of more than three Ub. Sequence analysis identified two potential Ub binding sites on a single α-helical surface within the coiled-coil region of the V domain. Mutation of these putative Ub binding sites inhibited polyUb binding to the isolated V domain in vitro and impaired budding of lentiviruses. These data reveal an important role for K63 polyUb binding by ALIX in retroviral release.
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Base de dados:
MEDLINE
Assunto principal:
Retroviridae
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Proteínas de Ligação ao Cálcio
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HIV-1
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Vírus da Anemia Infecciosa Equina
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Proteínas de Ciclo Celular
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Ubiquitina
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Complexos Endossomais de Distribuição Requeridos para Transporte
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Liberação de Vírus
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article