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Science 8 February 1991:
Vol. 251. no. 4994, pp. 665 - 668
DOI: 10.1126/science.1846977
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Articles

Science, Vol 251, Issue 4994, 665-668
Copyright © 1991 by American Association for the Advancement of Science

articles

Fibroblast growth factor receptors from liver vary in three structural domains

JZ Hou, MK Kan, K McKeehan, G McBride, P Adams, and WL McKeehan

W. Alton Jones Cell Science Center, Inc., Lake Placid, NY 12946.

Changes in heparin-binding fibroblast growth factor gene expression and receptor phenotype occur during liver regeneration and in hepatoma cells. The nucleotide sequence of complementary DNA predicts that three amino-terminal domain motifs, two juxtamembrane motifs, and two intracellular carboxyl-terminal domain motifs combine to form a minimum of 6 and potentially 12 homologous polypeptides that constitute the growth factor receptor family in a single human liver cell population. Amino-terminal variants consisted of two transmembrane molecules that contained three and two immunoglobulin-like disulfide loops, as well as a potential intracellular form of the receptor. The two intracellular juxtamembrane motifs differed in a potential serine-threonine kinase phosphorylation site. One carboxyl-terminal motif was a putative tyrosine kinase that contained potential tyrosine phosphorylation sites. The second carboxyl-terminal motif was probably not a tyrosine kinase and did not exhibit the same candidate carboxyl-terminal tyrosine phosphorylation sites.


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