Higher‐order oligomerization promotes localization of SPOP to liquid nuclear speckles
| العنوان: | Higher‐order oligomerization promotes localization of SPOP to liquid nuclear speckles |
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| المؤلفون: | Gilbert G. Privé, Jihun Lee, Sophia A. Kenrick, Tanja Mittag, Michal Sharon, Peter Schuck, Melissa R. Marzahn, Suresh Marada, Huaying Zhao, Wesley J. Errington, Regina-Maria Kolaitis, Stacey K. Ogden, Gili Ben-Nissan, Stanley Pounds, Jennifer L. Peters, Amanda Nourse, J. Paul Taylor |
| المصدر: | The EMBO Journal |
| بيانات النشر: | John Wiley and Sons Inc., 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, Macromolecular Substances, membrane‐less organelle, speckle‐type POZ protein, Mutant, Kruppel-Like Transcription Factors, Nerve Tissue Proteins, SPOP, Oligomer, ubiquitin ligase, General Biochemistry, Genetics and Molecular Biology, Article, 03 medical and health sciences, chemistry.chemical_compound, Ubiquitin, Protein Domains, Structural Biology, Zinc Finger Protein Gli3, Organelle, medicine, isodesmic self‐association, Humans, Molecular Biology, Cell Nucleus, 030102 biochemistry & molecular biology, General Immunology and Microbiology, biology, General Neuroscience, Ubiquitination, RNA, Post-translational Modifications, Proteolysis & Proteomics, Nuclear Proteins, Articles, Protein Biosynthesis & Quality Control, prostate cancer, Ubiquitin ligase, Repressor Proteins, 030104 developmental biology, medicine.anatomical_structure, chemistry, Biochemistry, biology.protein, Biophysics, Protein Multimerization, Nucleus, Protein Binding |
| الوصف: | Membrane‐less organelles in cells are large, dynamic protein/protein or protein/RNA assemblies that have been reported in some cases to have liquid droplet properties. However, the molecular interactions underlying the recruitment of components are not well understood. Herein, we study how the ability to form higher‐order assemblies influences the recruitment of the speckle‐type POZ protein (SPOP) to nuclear speckles. SPOP, a cullin‐3‐RING ubiquitin ligase (CRL3) substrate adaptor, self‐associates into higher‐order oligomers; that is, the number of monomers in an oligomer is broadly distributed and can be large. While wild‐type SPOP localizes to liquid nuclear speckles, self‐association‐deficient SPOP mutants have a diffuse distribution in the nucleus. SPOP oligomerizes through its BTB and BACK domains. We show that BTB‐mediated SPOP dimers form linear oligomers via BACK domain dimerization, and we determine the concentration‐dependent populations of the resulting oligomeric species. Higher‐order oligomerization of SPOP stimulates CRL3 SPOP ubiquitination efficiency for its physiological substrate Gli3, suggesting that nuclear speckles are hotspots of ubiquitination. Dynamic, higher‐order protein self‐association may be a general mechanism to concentrate functional components in membrane‐less cellular bodies. |
| اللغة: | English |
| تدمد: | 1460-2075 0261-4189 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d98ac140a585464c6be21774026e4b9Test http://europepmc.org/articles/PMC4910529Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....0d98ac140a585464c6be21774026e4b9 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14602075 02614189 |
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