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SAM as a protein interaction domain involved in developmental regulation
J Schultz1, C P Ponting, K Hofmann
1EMBL, Heidelberg, Germany.
Protein Science : a Publication of the Protein Society
|January 1, 1997
Summary
New protein discovery reveals the evolutionarily conserved SAM domain
Area of Science:
- Biochemistry
- Molecular Biology
- Developmental Biology
Background:
- The SAM (Sterile Alpha Motif) domain is a protein-protein interaction module implicated in various cellular functions.
- Previous studies have identified a limited number of SAM domain-containing proteins, hindering a comprehensive understanding of their roles.
Purpose of the Study:
- To identify novel SAM domain-containing proteins using advanced computational methods.
- To investigate the evolutionary conservation and functional implications of the SAM domain.
Main Methods:
- Utilized profile searching methods to screen protein databases for SAM domain homology.
- Bioinformatic analysis was employed to identify and categorize newly discovered SAM domain proteins.
Main Results:
- Identified over 60 previously undetected SAM domain-containing proteins.
- This cohort includes over 40 EPH-related receptor tyrosine kinases (RPTK), Drosophila bicaudal-C, a p53 from Loligo forbesi, and diacylglycerol-kinase isoform delta.
- A conserved tyrosine residue within the SAM domain of EPH-related RPTKs was identified, suggesting a role in signal transduction.
Conclusions:
- The SAM domain is an evolutionarily conserved module involved in regulating diverse developmental processes across eukaryotes.
- The identified conserved tyrosine in EPH RPTKs likely mediates cell-cell signaling through SH2 domain-containing protein interactions with phosphotyrosine.