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(Received for publication, January 29, 1997, and in revised form, February 18, 1997)
From the Raf-1 is a major downstream effector of mammalian
Ras. Binding of the effector domain of Ras to the Ras-binding domain of Raf-1 is essential for Ras-dependent Raf-1 activation.
However, Rap1A, which has an identical effector domain to that of Ras, cannot activate Raf-1 and even antagonizes several Ras functions in vivo. Recently, we identified the cysteine-rich region
(CRR) of Raf-1 as another Ras-binding domain. Ha-Ras proteins carrying mutations N26G and V45E, which failed to bind to CRR, also failed to
activate Raf-1. Since these mutations replace Ras residues with those
of Rap1A, we examined if Rap1A lacks the ability to bind to CRR.
Contrary to the expectation, Rap1A exhibited a greatly enhanced binding
to CRR compared with Ha-Ras. Enhanced CRR binding was also found with
Ha-Ras carrying another Rap1A-type mutation E31K. Both Rap1A and
Ha-Ras(E31K) mutant failed to activate Raf-1 and interfered with
Ha-Ras-dependent activation of Raf-1 in Sf9 cells. Enhanced
binding of Rap1A to CRR led to co-association of Rap1A and Ha-Ras with
Raf-1 N-terminal region through binding to CRR and Ras-binding domain,
respectively. These results suggest that Rap1A interferes with
Ras-dependent Raf-1 activation by inhibiting binding of Ras
to Raf-1 CRR.
Volume 272, Number 18,
Issue of May 2, 1997
pp. 11702-11705
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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