Exploiting the kinesin-1 molecular motor to generate a virus membrane penetration site.
Nat Commun
; 8: 15496, 2017 05 24.
Article
em En
| MEDLINE
| ID: mdl-28537258
ABSTRACT
Viruses exploit cellular machineries to penetrate a host membrane and cause infection, a process that remains enigmatic for non-enveloped viruses. Here we probe how the non-enveloped polyomavirus SV40 penetrates the endoplasmic reticulum (ER) membrane to reach the cytosol, a crucial infection step. We find that the microtubule-based motor kinesin-1 is recruited to the ER membrane by binding to the transmembrane J-protein B14. Strikingly, this motor facilitates SV40 ER-to-cytosol transport by constructing a penetration site on the ER membrane called a 'focus'. Neither kinesin-2, kinesin-3 nor kinesin-5 promotes foci formation or infection. The specific use of kinesin-1 is due to its unique ability to select posttranslationally modified microtubules for cargo transport and thereby spatially restrict focus formation to the perinucleus. These findings support the idea of a 'tubulin code' for motor-dependent trafficking and establish a distinct kinesin-1 function in which a motor is exploited to create a viral membrane penetration site.
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Base de dados:
MEDLINE
Assunto principal:
Cinesinas
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Vírus 40 dos Símios
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Retículo Endoplasmático
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Internalização do Vírus
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Membranas Intracelulares
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article