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Biochem Biophys Res Commun. 1994 Sep 30;203(3):1589-98.

Nuclear localization of p185neu tyrosine kinase and its association with transcriptional transactivation.

Author information

1
Department of Tumor Biology, University of Texas M. D. Anderson Cancer Center, Houston 77030.

Abstract

The rat neu protooncogene encodes a 185 kD transmembrane protein (p185neu), which is a member of the epidermal growth factor receptor (EGFr) family. In searching for the signaling transducer of p185neu by using a two-hybrid selection system, we found, surprisingly, that the cytoplasmic domain of p185neu, when fused to the DNA-binding domain of GAL4 (amino acids 1-147), functioned as a transcriptional activator. We subsequently observed nuclear localization of p185neu. Interestingly, nuclear p185neu has a much higher extent of tyrosine phosphorylation than its nonnuclear counterpart. Our results suggest that a transmembrane receptor tyrosine kinase may enter the nucleus and be involved in transcriptional activation. This novel finding unveils a clue in the understanding of the mechanism of receptor tyrosine kinase-mediated signal transduction.

PMID:
7945309
DOI:
10.1006/bbrc.1994.2368
[Indexed for MEDLINE]

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