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J Biol Chem, Vol. 275, Issue 19, 14124-14131, May 12, 2000
From the Department of Molecular, Cellular, and Developmental
Biology, and the Neuroscience Research Institute, University of
California, Santa Barbara, California 93106
Transforming growth factor-
Primary Structure Requirements for Xenopus
Nodal-related 3 and a Comparison with Regions Required by
Xenopus Nodal-related 2*
superfamily
members play important roles in the early development of animals.
Activin and the Xenopus nodal related proteins 1, 2, and 4 induce muscle actin from Xenopus ectodermal explants,
whereas the bone morphogenetic proteins 4 and 7 induce ectoderm to
differentiate as epidermis. Bone morphogenetic proteins are antagonized
by soluble binding proteins such as noggin and chordin, which leads to
expression of neural cell adhesion molecule in animal caps. The
transforming growth factor- superfamily member Xenopus
nodal-related 3 also induces the neural cell adhesion molecule through
inhibition of bone morphogenetic proteins. Therefore, whereas
Xenopus nodal-related 2 and 3 share a high amount of
sequence homology, they lead to very different cell fates. This study
investigates the functional domains that distinguish the activities of
these two factors. It was found that mutually exclusive regions of
nodal-related 2 and 3 were required for activity. The central region of
the mature domain is required for nodal-related 2 to induce muscle actin, whereas the N- and C-terminal ends of the mature domain are
required for nodal-related 3 to induce neural cell adhesion molecule.
These results help to define the minimal domains required for the
unique activities of these factors.
*
This work was supported by Grant GM52835 from the National
Institutes of Health and the Beckman Young Investigators Program (to
W. C. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: (805) 893-7698;
Fax: (805) 893-2005; E-mail: w_smith@lifesci.ucsb.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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