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Multiple mRNAs code for proteins related to the BEK fibroblast growth factor receptor
P Champion-Arnaud1, C Ronsin, E Gilbert
1Faculté des Sciences, Université de Nantes, France.
Abstract:
The BEK transmembrane protein tyrosine kinase is a receptor for both acidic and basic fibroblast growth factors. We identify several different transcripts which code for BEK-related proteins. These proteins differ from BEK in regions expected to control receptor activity. Thus, some of the proteins have altered extracellular, ligand-binding domains, and others an altered carboxy-terminal tail. Still other forms of BEK differ only in their juxtamembrane domains. Sequencing of parts of the BEK gene shows that alternative splicing of the premessenger can account for at least some of this diversity. In particular, an apparently tissue specific, mutually exclusive splicing of two internal exons permits both the previously described K-SAM mRNA and the BEK mRNA to be derived from the same premessenger.
Insights
The BEK receptor tyrosine kinase and related proteins are generated from a single gene through alternative splicing. This process creates diverse protein forms with altered functional domains, impacting fibroblast growth factor signaling.
Area of Science:
- Molecular Biology
- Cell Signaling
- Genetics
Background:
- The BEK receptor tyrosine kinase binds fibroblast growth factors, mediating crucial cellular processes.
- Understanding the diversity of BEK-related proteins is essential for comprehending growth factor signaling pathways.
Purpose of the Study:
- To identify and characterize different transcripts encoding BEK-related proteins.
- To investigate the molecular mechanisms generating BEK protein diversity.
Main Methods:
- Transcript identification and sequencing.
- Analysis of gene structure and alternative splicing.
- Protein domain analysis.
Main Results:
- Several BEK-related transcripts coding for proteins with altered domains (extracellular, carboxy-terminal, juxtamembrane) were identified.
- Alternative splicing of the BEK gene premessenger accounts for this diversity.
- Tissue-specific, mutually exclusive splicing generates distinct BEK and K-SAM mRNAs from the same precursor.
Conclusions:
- Alternative splicing is a key mechanism generating functional diversity in BEK receptor tyrosine kinase signaling.
- The identified BEK variants may possess distinct ligand-binding or signaling properties.
- This molecular mechanism provides a basis for tissue-specific regulation of fibroblast growth factor responses.