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J Biol Chem, Vol. 274, Issue 21, 14706-14715, May 21, 1999
From the a Kimmel Cancer Center, Thomas Jefferson
University, Philadelphia, Pennsylvania 19107, the
f Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, the
h Albert Einstein College of Medicine, New York, and
i The Molecular Sciences Institute,
Berkeley, California 94704
Tvl-1 is a 269-amino acid ankyrin repeat protein
expressed primarily in thymus, lung, and testes that was identified by
screening a murine T-cell two-hybrid cDNA library for proteins that
associate with the serine-threonine kinase Raf-1. The interaction of
Tvl-1 with Raf-1 was confirmed by co-immunoprecipitation of the two proteins from COS-1 cells transiently transfected with Tvl-1 and Raf-1
expression constructs as well as by co-immunoprecipitation of the
endogenous proteins from CV-1 and NB2 cells. Tvl-1 interacts with Raf-1
via its carboxyl-terminal ankyrin repeat domain. The same domain also
mediates Tvl-1 homodimerization. Tvl-1 was detected by
immunofluorescence in both the cytoplasm and the nucleus suggesting that in addition to Raf-1 it may also interact with nuclear proteins. Activated Raf-1 phosphorylates Tvl-1 both in vitro and
in vivo. In baculovirus-infected Sf9 insect cells,
Tvl-1 potentiates the activation of Raf-1 by Src and Ras while in COS-1
cells it potentiates the activation of Raf-1 by EGF. These data suggest
that Tvl-1 is both a target as well as a regulator of Raf-1. The human
homologue of Tvl-1 maps to chromosome 19p12, upstream of
MEF2B with the two genes in a head to head arrangement.
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