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J Biol Chem, Vol. 274, Issue 21, 14525-14528, May 21, 1999
From the Department of Pharmacy, University of Sydney, New South
Wales 2006, Australia
Ral-A is a Ras-related GTP-binding protein that
has been suggested to be the downstream target of Ras proteins and is
involved in the tyrosine kinase-mediated, Ras-dependent
activation of phospholipase D. We reported recently that Ral-A purified
from human erythrocyte membrane binds to calmodulin in a
Ca2+-dependent manner at a calmodulin
binding domain identified near its C-terminal region (Wang, K. L.,
Khan, M. T., and Roufogalis, B. D. (1997) J. Biol.
Chem. 272, 16002-16009). In this study we show the enhancement
of GTP binding to Ral-A by Ca2+/calmodulin. The stimulation
up to 3-fold by calmodulin was Ca2+-dependent,
with half-maximum activation occurring at 180 nM calmodulin and 80 nM free Ca2+ concentration. The present
work supports a regulatory role of Ca2+/calmodulin for the
activation of Ral-A and suggests a possible direct link between signal
transduction pathways of Ca2+/calmodulin and Ral-A proteins.
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