Nucleic Acids Research, Vol 24, Issue 20 4050-4056, Copyright © 1996 by Oxford University Press
JL Reiter and NJ Maihle
The epidermal growth factor receptor (EGFR) is encoded by the c-erbB1
proto-oncogene and plays an important role in the control of cell growth
and differentiation. To study the potential growth regulatory role of
soluble EGF receptors, we have isolated cDNA clones encoding a truncated,
secreted form of the human EGFR. The 5' sequence of this cDNA is identical
to the EGFR transcript encoding the full-length receptor through exon 10.
The unique 3' sequence encodes two additional amino acid residues before
encountering an in-frame stop codon, a poly(A) addition site and a poly(A)+
tail. Sequence comparison with genomic DNA sequences demonstrates that this
alternative transcript arises by read-through of a splice donor site. As a
result, this transcript encodes a portion of the extracellular
ligand-binding domain, but lacks the transmembrane domain and the
intracellular tyrosine kinase catalytic domain present in the EGFR.
Conditioned medium from transfected fibroblast cells contains a 60 kDa
protein that is specifically immunoprecipitated by an EGFR monoclonal
antibody. These findings demonstrate that alternative processing of the
human EGFR transcript produces a secreted product composed of only the
extracellular ligand-binding domain.
ARTICLES
A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor
Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
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