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Verfasst von:Pan, Xiaoyu [VerfasserIn]   i
 Geist, Miriam M. [VerfasserIn]   i
 Rudolph, Jochen M. [VerfasserIn]   i
 Nickel, Walter [VerfasserIn]   i
 Fackler, Oliver Till [VerfasserIn]   i
Titel:HIV-1 Nef disrupts membrane-microdomain-associated anterograde transport for plasma membrane delivery of selected Src family kinases
Verf.angabe:Xiaoyu Pan, Miriam M. Geist, Jochen M. Rudolph, Walter Nickel and Oliver T. Fackler
E-Jahr:2013
Jahr:18 April 2013
Umfang:17 S.
Fussnoten:Gesehen am 16.12.2021
Titel Quelle:Enthalten in: Cellular microbiology
Ort Quelle:Oxford [u.a.] : Wiley-Blackwell, 1999
Jahr Quelle:2013
Band/Heft Quelle:15(2013), 10, Seite 1605-1621
ISSN Quelle:1462-5822
Abstract:HIV-1 Nef, an essential factor in AIDS pathogenesis, boosts virus replication in vivo. As one of its activities in CD4+ T-lymphocytes, Nef potently retargets the Src family kinase (SFK) Lck but not closely related Fyn from the plasma membrane to recycling endosomes and the trans-Golgi network to tailor T-cell activation and optimize virus replication. Investigating the underlying mechanism we find Lck retargeting involves removal of the kinase from membrane microdomains. Moreover, Nef interferes with rapid vesicular transport of Lck to block anterograde transport and plasma membrane delivery of newly synthesized Lck. The sensitivity of Lck to Nef does not depend on functional domains of Lck but requires membrane insertion of the kinase. Surprisingly, the short N-terminal SH4 domain membrane anchor of Lck is necessary and sufficient to confer sensitivity to Nef-mediated anterograde transport block and microdomain extraction. In contrast, the SH4 domain of Fyn is inert to Nef-mediated manipulation. Nef thus interferes with a specialized membrane microdomain-associated pathway for plasma membrane delivery of newly synthesized Lck whose specificity is determined by the affinity of cargo for these sorting platforms. These results provide new insight into the mechanism of Nef action and the pathways used for SFK plasma membrane delivery.
DOI:doi:10.1111/cmi.12148
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1111/cmi.12148
 Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/cmi.12148
 DOI: https://doi.org/10.1111/cmi.12148
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1782361871
Verknüpfungen:→ Zeitschrift

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