tetano
Editor, Senior Moderator
FEBS Lett. 2012 Jan 10. [Epub ahead of print]
Mutation of a raft-targeting signal in the transmembrane region retards transport of influenza virus hemagglutinin through the Golgi.
Engel S, de Vries M, Herrmann A, Veit M.
Source
Immunology and Molecular Biology, Veterinary Medicine Faculty, Free University, Berlin, Germany.
Abstract
Inclusion of proteins into membrane-rafts favours interactions required for virus assembly but has also been proposed to facilitate vesicular transport of proteins. The hemagglutinin (HA) of influenza virus contains a raft-targeting sequence in the outer leaflet of its transmembrane region. We report that its mutation enhances co-localization of HA with a cis-Golgi marker and retards Golgi-localized processing, such as acquisition of Endo-H resistant carbohydrates and proteolytic cleavage. In contrast, trimerization of the molecule in the ER and transport to the apical membrane were not affected. The second signal for raft-targeting, S-acylation at cytoplasmic cysteines, did not retard HA transport.
Copyright ? 2012. Published by Elsevier B.V.
PMID:
22245151
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22245151
Mutation of a raft-targeting signal in the transmembrane region retards transport of influenza virus hemagglutinin through the Golgi.
Engel S, de Vries M, Herrmann A, Veit M.
Source
Immunology and Molecular Biology, Veterinary Medicine Faculty, Free University, Berlin, Germany.
Abstract
Inclusion of proteins into membrane-rafts favours interactions required for virus assembly but has also been proposed to facilitate vesicular transport of proteins. The hemagglutinin (HA) of influenza virus contains a raft-targeting sequence in the outer leaflet of its transmembrane region. We report that its mutation enhances co-localization of HA with a cis-Golgi marker and retards Golgi-localized processing, such as acquisition of Endo-H resistant carbohydrates and proteolytic cleavage. In contrast, trimerization of the molecule in the ER and transport to the apical membrane were not affected. The second signal for raft-targeting, S-acylation at cytoplasmic cysteines, did not retard HA transport.
Copyright ? 2012. Published by Elsevier B.V.
PMID:
22245151
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22245151