Work

SAM as a protein interaction domain involved in developmental regulation

Year: 1997

Type: article

Abstract: 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 diacyglycerol-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.

Source: Protein Science

DOI: 10.1002/pro.5560060128

Authors: Jörg Schultz, Peer Bork, Christopher P. Ponting, Kay Hofmann

Institutions: European Molecular Biology Laboratory, Max Delbrück Center, University of Oxford, ISREC Foundation

Language: English

Topic: Axon Guidance and Neuronal Signaling

Subfield: Cellular and Molecular Neuroscience

Field: Neuroscience

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2103785126

FWCI: 5.707

Cites: 38

Cited by: 306

Related to: 10