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J. Biol. Chem., Vol. 268, Issue 30, 22259-22261, 10, 1993
S Kishida, H Shirataki, T Sasaki, M Kato, K Kaibuchi and Y Takai
Rabphilin-3A is a putative target protein for Rab3A, a member of the small
G protein superfamily that is implicated in regulated secretion,
particularly in neurotransmitter release. Rabphilin-3A contains at least
two functionally different domains: the N-terminal Rab3A-binding domain and
the C-terminal C2 domain, which interacts with both Ca2+ and phospholipid.
Because Rabphilin-3A interacts preferentially with GTP- Rab3A rather than
with GDP-Rab3A, we have examined here whether Rabphilin-3A affects the
GTPase activity of Rab3A. Rabphilin-3A and its N-terminal fragment, but not
its C-terminal fragment, very weakly stimulated the basal GTPase activity
of Rab3A. However, Rabphilin-3A and its N-terminal fragment strongly
inhibited the Rab3A GAP-stimulated GTPase activity of Rab3A. Ca2+ and
phospholipid showed no effect on these activities of Rabphilin-3A. The
physiological significance of the GAP activity of Rabphilin-3A is obscure,
but it is likely that Rabphilin-3A inhibits Rab3A GAP activity and keeps
Rab3A in the GTP- bound active form during its action as a target molecule
for Rab3A.
Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein
Department of Biochemistry, Kobe University School of Medicine, Japan.
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