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J Biol Chem, Vol. 274, Issue 27, 19025-19034, July 2, 1999
From the Signal Transduction Laboratory, Institute of Molecular and
Cell Biology, National University of Singapore, 30 Medical Drive,
Singapore 117609, Republic of Singapore
FRS2 is a docker protein that recruits signaling
proteins to the plasma membrane in fibroblast growth factor signal
transduction. We report here that FRS2 was associated with PKC 
when
Swiss 3T3 cells were stimulated with basic fibroblast growth factor. PKC 
, the other member of the atypical PKC subfamily, could also bind FRS2. The association between FRS2 and PKC is likely to be
direct as shown by yeast two-hybrid analysis. The C-terminal fragments
of FRS2 (amino acid residues 300-508) and SNT2 (amino acids 281-492),
an isoform bearing 50% identity to FRS2, interacted with PKC at a
region (amino acids 240-562) that encompasses the catalytic domain.
In vitro kinase assays revealed neither FRS2 nor SNT2 was a
substrate of PKC or . Mutation of the alanine residue (Ala-120)
to glutamate in the pseudo-substrate region of PKC results in a
constitutively active kinase that exhibited more than 2-fold greater
binding to FRS2 in vitro than its "closed" wild-type
counterpart. Tyrosine phosphorylation of FRS2 did not affect its
binding to the constitutively active PKC mutant, suggesting that
the activation of PKC is necessary and sufficient for its
association with FRS2. It is likely that FRS2 serves as an anchoring
protein for targeting activated atypical PKCs to the cell plasma
membrane in signaling pathways.
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