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J Biol Chem, Vol. 274, Issue 17, 11796-11810, April 23, 1999
From the Division of Biochemistry & Molecular Biology, IBLS,
Davidson Building, University of Glasgow,
Glasgow G12 8QQ, Scotland, United Kingdom
The cAMP-specific phosphodiesterase (PDE)
HSPDE 4A4B(pde46) selectively bound SH3 domains of SRC family
tyrosyl kinases. Such an interaction profoundly changed the inhibition
of PDE4 activity caused by the PDE4-selective inhibitor rolipram and
mimicked the enhanced rolipram inhibition seen for particulate,
compared with cytosolic pde46 expressed in COS7 cells. Particulate
pde46 co-localized with LYN kinase in COS7 cells. The unique N-terminal
and LR2 regions of pde46 contained the sites for SH3 binding. Altered
rolipram inhibition was triggered by SH3 domain interaction with the
LR2 region. Purified LYN SH3 and human PDE4A LR2 could be
co-immunoprecipitated, indicating a direct interaction. Protein kinase
A-phosphorylated pde46 remained able to bind LYN SH3. pde46 was found
to be associated with SRC kinase in the cytosol of COS1 cells, leading
to aberrant kinetics of rolipram inhibition. It is suggested that pde46
may be associated with SRC family tyrosyl kinases in intact cells and
that the ensuing SH3 domain interaction with the LR2 region of pde46
alters the conformation of the PDE catalytic unit, as detected by
altered rolipram inhibition. Interaction between pde46 and SRC family
tyrosyl kinases highlights a potentially novel regulatory system and
point of signaling system cross-talk.
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