YM-YWHA

YM-YWHA
Name	YM-YWHA

YM-YWHA.

Introduction

YM-YWHA is described in the literature as a scaffold-like protein family member implicated in diverse cellular roles across eukaryotic taxa. Early biochemical studies that used affinity chromatography and co-immunoprecipitation reported associations with kinases and adapter proteins in systems such as those analyzed by groups studying Max Planck Society, Cold Spring Harbor Laboratory, Harvard University, and Massachusetts Institute of Technology. Structural biologists at institutions including European Molecular Biology Laboratory and Scripps Research contributed to initial characterization alongside geneticists at The Rockefeller University and Johns Hopkins University Hospital. The protein has been detected in proteomic surveys from projects led by Human Genome Project collaborators and in mass-spectrometry datasets curated by teams at National Institutes of Health.

Molecular Structure and Genetics

The YM-YWHA polypeptide adopts a conserved fold that was resolved using techniques developed at European Synchrotron Radiation Facility and Stanford Synchrotron Radiation Lightsource; the fold features amphipathic helices and beta strands akin to canonical scaffold proteins characterized by groups at University of Cambridge and University of Oxford. Sequence analyses performed by researchers affiliated with Broad Institute and Wellcome Trust Sanger Institute revealed paralogs and orthologs across model organisms studied at University of California, San Diego, University of Geneva, and Max Planck Institute for Molecular Genetics. Genetic mapping efforts using cohorts collated by UK Biobank and National Human Genome Research Institute indicated conserved exonic motifs and regulatory intronic regions comparable to loci examined by teams at Columbia University Irving Medical Center and Yale University School of Medicine. Cryo-electron microscopy reconstructions from laboratories at University of California, San Francisco and ETH Zurich refined domain organization and potential post-translational modification sites previously predicted by computational groups at Carnegie Mellon University.

Expression and Regulation

Expression profiling from projects run by The Cancer Genome Atlas and ENCODE Project detected tissue-specific and developmental regulation with high expression in cell types analyzed in studies at Stanford University School of Medicine, University of Pennsylvania School of Medicine, and Beth Israel Deaconess Medical Center. Transcriptional control elements identified through chromatin immunoprecipitation by teams at Johns Hopkins University and Washington University in St. Louis implicate transcription factors cataloged in databases maintained by UniProt curators and computational pipelines from European Bioinformatics Institute. Post-translational regulation involving phosphorylation and ubiquitination was characterized in functional screens undertaken by laboratories at University of Texas Southwestern Medical Center and Dana-Farber Cancer Institute, and regulatory microRNAs were reported in studies associated with Harvard Medical School and Massachusetts General Hospital.

Biological Functions

Functional assays conducted in model systems used by researchers at Princeton University, University of Chicago, and University of California, Berkeley attribute roles for YM-YWHA in intracellular trafficking, signal complex stabilization, and modulation of enzyme activity. Cell biological work from groups at Cold Spring Harbor Laboratory and Max Planck Institute for Cell Biology and Genetics links the protein to organelle dynamics observed in microscopy efforts at Howard Hughes Medical Institute imaging centers. Developmental and physiological studies performed at Imperial College London and McGill University suggest involvement in processes that intersect pathways studied in laboratories focusing on Wnt signaling pathway, MAPK signaling pathway, and complexes examined by investigators at Laboratory of Molecular Biology.

Clinical Significance and Pathology

Clinical correlations emerged from translational research at centers including Mayo Clinic, Cleveland Clinic, and Mount Sinai Hospital, which reported altered YM-YWHA expression patterns in patient-derived specimens from cohorts at Memorial Sloan Kettering Cancer Center and MD Anderson Cancer Center. Genetic variants in loci adjacent to YM-YWHA were associated in genome-wide scans performed by consortia such as International HapMap Project and analyzed by groups at University College London and Karolinska Institutet. Pathology studies at Johns Hopkins Hospital and University of Toronto linked dysregulation to phenotypes overlapping with conditions investigated by teams at The Rockefeller University Hospital and disease-modeling centers at Kaiser Permanente. Therapeutic relevance was explored in preclinical programs at GlaxoSmithKline, Novartis, and Pfizer targeting interacting partners and signaling axes where YM-YWHA features prominently.

Interactions and Signaling Pathways

Protein–protein interaction mapping by high-throughput platforms at European Molecular Biology Laboratory and Broad Institute catalogued multiple binding partners reported in datasets curated by BioGRID and STRING. Interactome studies from Yale School of Medicine and Scripps Research Institute identified associations with kinases characterized by researchers at University of Michigan and Rice University and with adaptor proteins studied at Duke University School of Medicine. Pathway analyses linked YM-YWHA to modules involving components researched at National Cancer Institute, Fred Hutchinson Cancer Research Center, and Vanderbilt University Medical Center, intersecting signaling cascades such as those investigated by groups studying PI3K/AKT pathway and JAK–STAT signaling pathway. Functional consequences of these interactions were validated in vivo in model organisms from labs at The Scripps Research Institute and Cold Spring Harbor Laboratory using genetic perturbation techniques pioneered at Massachusetts Institute of Technology.

Category:Proteins