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Journal of Cell Science, Vol 102, Issue 4 739-752, Copyright © 1992 by Company of Biologists
JOURNAL ARTICLES |
S Cheley, KS Kosik, P Paskevich, S Bakalis and H Bayley
Worcester Foundation for Experimental Biology, Shrewsbury, MA 01545.
Insect ovarian Sf9 cells extend processes with complex morphologies when infected with a recombinant baculovirus encoding the catalytic subunit of protein kinase A. Within the shafts of the processes are abundant microtubules, which, in contrast to those in Sf9 cells expressing the microtubule-associated protein tau, are generally not organized into parallel bundles. During infection the late viral polypeptide p10 becomes phosphorylated by the protein kinase A catalytic subunit at its penultimate residue, Ser92. The expression or phosphorylation of other major host cell or viral polypeptides does not change, compared with polypeptides from a wild-type viral infection. Once phosphorylated, p10 associates with microtubules in the infected cells and may thereby play a role in process formation.
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