The Many Faces of SAM

Feng Qiao and James U. Bowie^*

University of California, Los Angeles–U.S. Department of Energy (UCLA-DOE) Institute of Genomics and Proteomics, Molecular Biology Institute, Department of Chemistry and Biochemistry, UCLA, CA 90095, USA.

Abstract: Protein-protein interactions are essential for the assembly, regulation, and localization of functional protein complexes in the cell. SAM domains are among the most abundant protein-protein interaction motifs in organisms from yeast to humans. Although SAM domains adopt similar folds, they are remarkably versatile in their binding properties. Some identical SAM domains can interact with each other to form homodimers or polymers. In other cases, SAM domains can bind to other related SAM domains, to non–SAM domain–containing proteins, and even to RNA. Such versatility earns them functional roles in myriad biological processes, from signal transduction to transcriptional and translational regulation. In this review, we describe the structural basis of SAM domain interactions and highlight their roles in the scaffolding of protein complexes in normal and pathological processes.

*Corresponding author. Department of Chemistry and Biochemistry, Room 655, Boyer Hall, UCLA, 611 Charles E. Young Drive East, Los Angeles, CA 90095–1570, USA. E-mail: bowie{at}mbi.ucla.edu

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