title: The many faces of SAM.
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.
authors.affiliation: U.S. Department of Energy (UCLA-DOE) Institute of Genomics and Proteomics, Molecular Biology Institute, Department of Chemistry and Biochemistry, UCLA, CA 90095, USA.
authors.forename: Feng
authors.initials: F
authors.lastname: Qiao
authors.forename: James U
authors.initials: JU
authors.lastname: Bowie
mesh_terms: D000818:Animals; D001704:Biopolymers; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000502:physiology; D029721:Drosophila Proteins / Q000737:chemistry / Q000502:physiology; D005057:Eukaryotic Cells / Q000378:metabolism; D005136:Eye Proteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry / Q000502:physiology; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000502:physiology; D010766:Phosphorylation; D063150:Polycomb Repressive Complex 1; D063146:Polycomb-Group Proteins; D011485:Protein Binding; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D011494:Protein Kinases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000502:physiology; D050783:Proto-Oncogene Proteins c-ets / Q000737:chemistry / Q000502:physiology; D012313:RNA / Q000378:metabolism; D036081:Receptors, Eph Family / Q000737:chemistry; D012097:Repressor Proteins / Q000737:chemistry / Q000502:physiology; D015398:Signal Transduction; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D000097764:ETS Translocation Variant 6 Protein
chemical_list: D001704:Biopolymers; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D005136:Eye Proteins; D047908:Intracellular Signaling Peptides and Proteins; D009419:Nerve Tissue Proteins; D063150:Polycomb Repressive Complex 1; D063146:Polycomb-Group Proteins; D011494:Protein Kinases; D011518:Proto-Oncogene Proteins; D050783:Proto-Oncogene Proteins c-ets; D012313:RNA; D036081:Receptors, Eph Family; D012097:Repressor Proteins; D025841:Small Ubiquitin-Related Modifier Proteins; D014157:Transcription Factors; D000097764:ETS Translocation Variant 6 Protein; C076188:AOP protein, Drosophila; C066770:Pc protein, Drosophila; C428945:edl protein, Drosophila; C083884:pnt protein, Drosophila