ArticleHuman genetics2008
The Opitz syndrome gene product MID1 assembles a microtubule-associated ribonucleoprotein complex.
Article in Human genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 65 citations in OpenAlex.
- Data-driven model reveals increased stability of CAG-expanded huntingtin RNA due to MID1 binding.PLoS computational biology · 2026Article
- Heart failure caused by Opitz syndrome: a case report and literature review.BMC cardiovascular disorders · 2025Review
- TRIM Proteins and Antiviral Microtubule Reorganization: A Novel Component in Innate Immune Responses?Viruses · 2024Review
- Opitz GBBB syndrome with total anomalous pulmonary venous connection: A new MID1 gene variant.Molecular genetics & genomic medicine · 2023Article
- Familial and syndromic forms of arachnoid cyst implicate genetic factors in disease pathogenesis.Cerebral cortex (New York, N.Y. : 1991) · 2023Article
- It's a TRIM-endous view from the top: the varied roles of TRIpartite Motif proteins in brain development and disease.Frontiers in molecular neuroscience · 2023Review
- RNA-binding is an ancient trait of the Annexin family.Frontiers in cell and developmental biology · 2023Article
- Review
- Emerging Roles of the TRIM E3 Ubiquitin Ligases MID1 and MID2 in Cytokinesis.Frontiers in physiology · 2019Review
- Inhibition of the MID1 protein complex: a novel approach targeting APP protein synthesis.Cell death discovery · 2018Article
- MID1-PP2A complex functions as new insights in human lung adenocarcinoma.Journal of cancer research and clinical oncology · 2018Article
- Two Novel PathogenicMolecular syndromology · 2017Article
- Resveratrol induces dephosphorylation of Tau by interfering with the MID1-PP2A complex.Scientific reports · 2017Article
- Update on 13 Syndromes Affecting Craniofacial and Dental Structures.Frontiers in physiology · 2017Review
- Hedgehog-dependent E3-ligase Midline1 regulates ubiquitin-mediated proteasomal degradation of Pax6 during visual system development.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- MicroRNAs-Proteomic Networks Characterizing Human Medulloblastoma-SLCs.Stem cells international · 2016Article
- Adaptive responses of androgen receptor signaling in castration-resistant prostate cancer.Oncotarget · 2015Review
- Metformin anti-tumor effect via disruption of the MID1 translational regulator complex and AR downregulation in prostate cancer cells.BMC cancer · 2014Article
- Article
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Opitz BBB/G syndrome (OS) is a heterogenous malformation syndrome mainly characterised by hypertelorism and hypospadias. In addition, patients may present with several other defects of the ventral midline such as cleft lip and palate and congenital heart defects. The syndrome-causing gene encodes the X-linked E3 ubiquitin ligase MID1 that mediates ubiquitin-specific modification and degradation of the catalytic subunit of the translation regulator protein phosphatase 2A (PP2A). Here, we show that the MID1 protein also associates with elongation factor 1alpha (EF-1alpha) and several other proteins involved in mRNA transport and translation, including RACK1, Annexin A2, Nucleophosmin and proteins of the small ribosomal subunits. Mutant MID1 proteins as found in OS patients lose the ability to interact with EF-1alpha. The composition of the MID1 protein complex was determined by several independent methods: (1) yeast two-hybrid screening and (2) immunofluorescence, (3) a biochemical approach involving affinity purification of the complex, (4) co-fractionation in a microtubule assembly assay and (5) immunoprecipitation. Moreover, we show that the cytoskeleton-bound MID1/translation factor complex specifically associates with G- and U-rich RNAs and incorporates MID1 mRNA, thus forming a microtubule-associated ribonucleoprotein (RNP) complex. Our data suggest a novel function of the OS gene product in directing translational control to the cytoskeleton. The dysfunction of this mechanism would lead to malfunction of microtubule-associated protein translation and to the development of OS.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.