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Protein Science, Vol 6, Issue 1 249-253, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

SAM as a protein interaction domain involved in developmental regulation

J. SCHULTZ, C. P. PONTING, K. HOFMANN and P. BORK
EMBL, Heidelberg and Max-Delbruck-Center for Molecular Medicine, Berlin-Buch, Germany

More than 60 previously undetected SAM domain-containing proteins have been identified using profile searching methods. Among these are over 40 EPH-related receptor tyrosine kinases (RPTK), Drosophila bicaudal-C, a p53 from Loligo forbesi, and diacylglycerol-kinase isoform {delta}. This extended dataset suggests that SAM is an evolutionary conserved protein binding domain that is involved in the regulation of numerous developmental processes among diverse eukaryotes. A conserved tyrosine in the SAM sequences of the EPH related RPTKs is likely to mediate cell-cell initiated signal transduction via the binding of SH2 containing proteins to phosphotyrosine.
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