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| SMC1 | |
|---|---|
| Name | Structural maintenance of chromosomes protein 1 |
| Organism | Homo sapiens |
SMC1 SMC1 is a eukaryotic structural maintenance protein that participates in chromosomal cohesion, DNA repair, and genome organization. It functions within a multi-protein complex alongside factors implicated in mitosis, meiosis, and checkpoint signaling, and its dysfunction is associated with developmental syndromes and cancer. Major studies have connected SMC1 to pathways involving prominent figures and institutions in molecular biology research.
SMC1 is a member of the structural maintenance of chromosomes family studied by groups at institutions such as Max Planck Society, Cold Spring Harbor Laboratory, Broad Institute, Massachusetts Institute of Technology, and Harvard University. Historical landmarks in chromosome biology involving researchers from Cambridge University, University of California, Berkeley, Stanford University, Yale University, and Princeton University intersect with experimental work on SMC1. Key conferences where SMC1 data were presented include meetings of the American Society for Cell Biology, European Molecular Biology Organization, and the Gordon Research Conferences.
SMC1 possesses an antiparallel coiled-coil architecture with conserved ABC-like ATPase "head" domains, a central hinge region, and long coiled coils—structural themes elucidated by teams at European Molecular Biology Laboratory, University of Cambridge, and California Institute of Technology. Human SMC1 exists as paralogs/isoforms described in comparative genomics studies from groups at University of Tokyo, Max Planck Institute for Biochemistry, and Karolinska Institute. Structural insights derive from collaborations involving Protein Data Bank, EMBL-EBI, and cryo-EM efforts led by researchers affiliated with National Institutes of Health and Riken. The SMC1 hinge mediates dimerization with partner SMC proteins while the ATPase domains mediate conformational changes, a paradigm also characterized in studies at University of Oxford, University College London, and ETH Zurich.
SMC1 functions as a core subunit of the cohesin complex alongside components first described by laboratories at Nagoya University, University of California, San Francisco, and Institut Pasteur. Cohesin's roles in sister chromatid cohesion, chromatin looping, and transcriptional regulation link SMC1 to chromosomal events studied in model systems by investigators at Johns Hopkins University, University of Edinburgh, McGill University, Seoul National University, and Weizmann Institute of Science. Cohesin cooperates with regulatory factors such as proteins characterized in work from Oncogene-affiliated groups and genome conformation studies from Wellcome Sanger Institute and European Bioinformatics Institute. Functional assays performed using reagents from Addgene and guidance from databases maintained by National Center for Biotechnology Information have defined SMC1's partners and interactions.
SMC1 is implicated in homologous recombination and DNA double-strand break repair pathways researched at Cold Spring Harbor Laboratory, Fred Hutchinson Cancer Center, and Dana-Farber Cancer Institute. Phosphorylation of SMC1 in response to DNA damage was characterized in studies from Salk Institute and labs collaborating with National Cancer Institute investigators. Connections between SMC1 activity and tumor suppressors or oncogenes have been explored by consortia including The Cancer Genome Atlas and clinical teams at Memorial Sloan Kettering Cancer Center and Mayo Clinic. Research on replication stress and checkpoint signaling involving SMC1 references work tied to European Molecular Biology Laboratory, Imperial College London, and Vanderbilt University.
Post-translational modifications of SMC1—phosphorylation, acetylation, and ubiquitination—have been mapped in proteomics studies conducted at Max Delbrück Center, ProteomeXchange, and mass spectrometry facilities affiliated with University of Washington. Kinases and ubiquitin ligases that modify SMC1 were identified in screens carried out by groups at Columbia University, University of North Carolina, and Duke University Hospital. Regulatory interplay with chromatin remodelers and transcription factors has been examined in collaborations involving The Rockefeller University, University of Chicago, and Cornell University.
Germline and somatic variants affecting SMC1 are linked to developmental disorders and cancers described in clinical series from Great Ormond Street Hospital, Cleveland Clinic, University Hospital Heidelberg, and pediatric genetics consortia. Cohesinopathies with features reported in case reports from Children's Hospital of Philadelphia and Royal Children's Hospital implicate SMC1 perturbation. Large-scale genetic studies from GENCODE, 1000 Genomes Project, and ExAC have cataloged SMC1 variants; oncogenic associations have been integrated into clinical guidelines from American Society of Clinical Oncology and diagnostic pipelines used at Mayo Clinic Laboratories.
Functional conservation of SMC1 has been demonstrated in yeast, Drosophila, mouse, and zebrafish models worked on at Saccharomyces Genome Database-linked labs, European Molecular Biology Laboratory, Max Planck Institute for Molecular Genetics, University of Cambridge, and RIKEN Center for Developmental Biology. Mouse knockout and conditional alleles studied at Jackson Laboratory and developmental phenotyping from Wellcome Trust Sanger Institute corroborate essential roles in embryogenesis and meiosis. Genetic interaction maps and synthetic lethality screens involving SMC1 were produced by consortia including International Knockout Mouse Consortium and research teams at Broad Institute.
Category:Proteins