• Media type: E-Article
  • Title: Phosphorylated baculovirus p10 is a heat-stable microtubule-associated protein associated with process formation in Sf9 cells
  • Contributor: Cheley, Stephen; Kosik, Kenneth S.; Paskevich, Peter; Bakalis, Shelley; Bayley, Hagan
  • imprint: The Company of Biologists, 1992
  • Published in: Journal of Cell Science
  • Language: English
  • DOI: 10.1242/jcs.102.4.739
  • ISSN: 0021-9533; 1477-9137
  • Keywords: Cell Biology
  • Origination:
  • Footnote:
  • Description: <jats:title>ABSTRACT</jats:title> <jats:p>Insect ovarian Sf? 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.</jats:p>
  • Access State: Open Access