Abstract:
:Many studies have shown that phospholipase D (PLD) is activated by protein kinase C (PKC) in vivo and in vitro. In this study, a PLD isoform (rPLD1) was shown to bind to PKC-alpha in Rat1 fibroblasts treated with phorbol ester. The PKC-alpha binding domain of rPLD1 was localized to its N-terminus. The phospholipase was shown to become associated also with a 220-kDa protein (p220) in the fibroblasts and in Sf9 cells infected with recombinant baculovirus coding rPLD1. This interaction was increased by phorbol myristate acetate (PMA) treatment. p220 was phosphorylated on serine/threonine in PMA-stimulated Rat1 cells, and rPLD1 expressed in Sf9 cells was also serine/threonine phosphorylated in response to PMA treatment. These data suggest the PMA induces the formation of a RPLD1/PKC alpha/P220 complex in cells, some components of which undergo serine/threonine phosphorylation.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Min DS,Exton JHdoi
10.1006/bbrc.1998.8990subject
Has Abstractpub_date
1998-07-30 00:00:00pages
533-7issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(98)98990-2journal_volume
248pub_type
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