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Isolation of ret proto-oncogene cDNA with an amino-terminal signal sequence
1Laboratory of Experimental Pathology, Aichi Cancer Center Research Institute, Nagoya, Japan.
Abstract:
Our recent studies suggested that the ret proto-oncogene protein is a cell surface receptor with a tyrosine kinase domain. However, the sequence of its cDNA lacked an amino-terminal signal sequence characteristic of membrane proteins. In the present study we have isolated and sequenced an additional cDNA clone. The nucleotide sequence of the cDNA obtained indicated that the 5' terminal 330 nucleotides differs from the published sequence of the ret proto-oncogene. In addition, the sequence contains an open reading frame with an amino-terminal signal sequence.
Insights
Researchers identified a new ret proto-oncogene cDNA sequence. This revised sequence includes a crucial amino-terminal signal sequence, confirming its role as a cell surface receptor protein.
Area of Science:
- Molecular Biology
- Oncology
- Cell Biology
Background:
- The ret proto-oncogene protein functions as a cell surface receptor with tyrosine kinase activity.
- Previous cDNA sequences lacked a signal sequence, which is characteristic of membrane proteins.
Purpose of the Study:
- To investigate the discrepancy in the ret proto-oncogene cDNA sequence.
- To identify a functional cDNA clone encoding the ret proto-oncogene receptor.
Main Methods:
- Isolation and sequencing of an additional cDNA clone of the ret proto-oncogene.
- Comparative nucleotide sequence analysis.
Main Results:
- A novel cDNA clone was isolated and sequenced.
- The 5' terminal 330 nucleotides of the new sequence differ from the previously published ret proto-oncogene sequence.
- The newly identified sequence contains an open reading frame with an amino-terminal signal sequence.
Conclusions:
- The revised cDNA sequence provides evidence for the ret proto-oncogene as a membrane-bound cell surface receptor.
- This finding clarifies the molecular characteristics of the ret proto-oncogene protein.