rab5 GTPase regulates adenovirus endocytosis.
Adenovirus interaction with alphav integrins is important for virus entry. We have examined the effects of adenovirus attachment on intracellular signaling in HeLa cells, with an emphasis on pathways known to be activated following integrin interaction with other ligands. We found no evidence for [Ca(2+)](c)-mediated signaling or for tyrosine phosphorylation of pp125(FAK), p130(CAS), and paxillin. However, adenovirus attachment is known to activate phosphatidylinositol-3 kinase, which in turn may regulate endocytosis via rab5 GTPase. We found that adenovirus uptake was increased by overexpression of wild-type rab5 and decreased by dominant-negative rab5. These results indicate a role for rab5 in adenovirus entry.
Rauma
T
T
Department of Pharmacology, University of Oulu, 90220 Oulu, Finland.
Tuukkanen
J
J
Bergelson
J M
JM
Denning
G
G
Hautala
T
T
D000260:Adenoviruses, Human / Q000235:genetics / Q000502:physiology*; D004705:Endocytosis; D015967:Gene Expression Regulation, Viral; D018014:Gene Transfer Techniques; D006367:HeLa Cells; D006801:Humans; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism; D015398:Signal Transduction; D014162:Transfection; D014407:Tumor Cells, Cultured; D020696:rab5 GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*
D019000:Phosphotyrosine; D020696:rab5 GTP-Binding Proteins