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Vol. 13, Issue 4, 1252-1262, April 2002
in RBL-2H3 Cells
Institute for Cancer Studies, Birmingham University, Birmingham,
B15 2TA, United Kingdom
Phospholipase D (PLD) activity can be detected in response to many
agonists in most cell types; however, the pathway from receptor
occupation to enzyme activation remains unclear. In vitro PLD1b
activity is phosphatidylinositol 4,5-bisphosphate dependent via
an N-terminal PH domain and is stimulated by Rho, ARF, and PKC family
proteins, combinations of which cooperatively increase this activity.
Here we provide the first evidence for the in vivo regulation of PLD1b
at the molecular level. Antigen stimulation of RBL-2H3 cells induces
the colocalization of PLD1b with Rac1, ARF6, and PKC
at the plasma
membrane in actin-rich structures, simultaneously with cooperatively
increasing PLD activity. Activation is both specific and direct because
dominant negative mutants of Rac1 and ARF6 inhibit stimulated PLD
activity, and surface plasmon resonance reveals that the regulatory
proteins bind directly and independently to PLD1b. This also indicates
that PLD1b can concurrently interact with a member from each regulator
family. Our results show that in contrast to PLD1b's translocation to the plasma membrane, PLD activation is phosphatidylinositol
3-kinase dependent. Therefore, because inactive, dominant negative
GTPases do not activate PLD1b, we propose that activation results from phosphatidylinositol 3-kinase-dependent stimulation of Rac1,
ARF6, and PKC.
Corresponding author. E-mail address:
m.j.o.wakelam{at}bham.ac.uk.
*
Present address: Biological Sciences, Warwick University,
Coventry, CV4 7AL, United Kingdom.
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