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    Science. 1991 Feb 8;251(4994):665-8.

    Fibroblast growth factor receptors from liver vary in three structural domains.

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

    Source

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

    Abstract

    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.

    PMID:
    1846977
    [PubMed - indexed for MEDLINE]

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