[HTML][HTML] Dependence of phospholipase D1 multi-monoubiquitination on its enzymatic activity and palmitoylation

H Yin, Y Gui, G Du, MA Frohman, XL Zheng - Journal of biological chemistry, 2010 - ASBMB
Phospholipase D (PLD) is an important lipase in many cellular processes, including
vesicular trafficking, cell survival, and cell migration. In the present study, we show that
PLD1, but not PLD2, is posttranslationally modified by multi-monoubiquitination. Intriguingly,
suppression of lipase activity either by mutation of the HKD motif (PLD1 H896R, K898R, or
D903A) or the phosphatidylinositol 4, 5-bisphosphate binding motif (PLD1 R691G, R695G)
or through use of PLD-selective inhibitors impaired the ubiquitination of PLD1, although …