Structural basis for dimerization quality control.

BTB-POZ Domain / genetics F-Box Proteins / metabolism Humans Kelch-Like ECH-Associated Protein 1 / chemistry Models, Biological Models, Molecular Protein Binding Protein Folding Protein Multimerization Protein Stability Stem Cell Factor / metabolism Ubiquitination

Journal

Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462

Informations de publication

Date de publication:
10 2020
Historique:
received: 21 10 2019
accepted: 21 05 2020
pubmed: 21 8 2020
medline: 15 12 2020
entrez: 21 8 2020
Statut: ppublish

Résumé

Most quality control pathways target misfolded proteins to prevent toxic aggregation and neurodegeneration

Identifiants

DOI: 10.1038/s41586-020-2636-7 PMID: 32814905 PMC: PMC8024055
pubmed: 32814905
doi: 10.1038/s41586-020-2636-7
pii: 10.1038/s41586-020-2636-7
pmc: PMC8024055
mid: NIHMS1596857
doi:

Substances chimiques

F-Box Proteins 0
FBXL17 protein, human 0
KEAP1 protein, human 0
KITLG protein, human 0
Kelch-Like ECH-Associated Protein 1 0
Stem Cell Factor 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

452-456

Subventions

Organisme : Howard Hughes Medical Institute
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30 GM124169
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM124149
Pays : United States

Références

Balchin, D., Hayer-Hartl, M. & Hartl, F. U. In vivo aspects of protein folding and quality control. Science 353, aac4354 (2016).
pubmed: 27365453
Mena, E. L. et al. Dimerization quality control ensures neuronal development and survival. Science 362, eaap8236 (2018).
pubmed: 30190310
Gordley, R. M., Bugaj, L. J. & Lim, W. A. Modular engineering of cellular signaling proteins and networks. Curr. Opin. Struct. Biol. 39, 106–114 (2016).
pubmed: 27423114 pmcid: 5127285
Ji, A. X. & Privé, G. G. Crystal structure of KLHL3 in complex with Cullin3. PLoS ONE 8, e60445 (2013).
pubmed: 23573258 pmcid: 3616122
Zhuang, M. et al. Structures of SPOP–substrate complexes: insights into molecular architectures of BTB–Cul3 ubiquitin ligases. Mol. Cell 36, 39–50 (2009).
pubmed: 19818708 pmcid: 2847577
Cleasby, A. et al. Structure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDO. PLoS ONE 9, e98896 (2014).
pubmed: 24896564 pmcid: 4045772
Ghetu, A. F. et al. Structure of a BCOR corepressor peptide in complex with the BCL6 BTB domain dimer. Mol. Cell 29, 384–391 (2008).
pubmed: 18280243 pmcid: 2665293
McGourty, C. A. et al. Regulation of the CUL3 ubiquitin ligase by a calcium-dependent co-adaptor. Cell 167, 525–538 (2016).
pubmed: 27716508
Werner, A. et al. Cell-fate determination by ubiquitin-dependent regulation of translation. Nature 525, 523–527 (2015).
pubmed: 26399832 pmcid: 4602398
Jin, L. et al. Ubiquitin-dependent regulation of COPII coat size and function. Nature 482, 495–500 (2012).
pubmed: 22358839 pmcid: 3292188
Furukawa, M. & Xiong, Y. BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3–Roc1 ligase. Mol. Cell. Biol. 25, 162–171 (2005).
pubmed: 15601839 pmcid: 538799
Wakabayashi, N. et al. Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation. Nat. Genet. 35, 238–245 (2003).
pubmed: 14517554
Louis-Dit-Picard, H. et al. KLHL3 mutations cause familial hyperkalemic hypertension by impairing ion transport in the distal nephron. Nat. Genet. 44, 456–460 (2012).
pubmed: 22406640
Maerki, S. et al. The Cul3–KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis. J. Cell Biol. 187, 791–800 (2009).
pubmed: 19995937 pmcid: 2806313
Sumara, I. et al. A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells. Dev. Cell 12, 887–900 (2007).
pubmed: 17543862
Duan, S. et al. FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas. Nature 481, 90–93 (2012).
pubmed: 22113614 pmcid: 3344385
Tan, M. K., Lim, H. J., Bennett, E. J., Shi, Y. & Harper, J. W. Parallel SCF adaptor capture proteomics reveals a role for SCF
pubmed: 24035498 pmcid: 3981468
Yamamoto, M., Kensler, T. W. & Motohashi, H. The KEAP1–NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis. Physiol. Rev. 98, 1169–1203 (2018).
pubmed: 29717933
Zheng, N. et al. Structure of the Cul1–Rbx1–Skp1–F box
pubmed: 11961546
Xing, W. et al. SCF
pubmed: 23503662 pmcid: 3618506
Schulman, B. A. et al. Insights into SCF ubiquitin ligases from the structure of the Skp1–Skp2 complex. Nature 408, 381–386 (2000).
pubmed: 11099048
Bhattacharyya, M. et al. Molecular mechanism of activation-triggered subunit exchange in Ca
pubmed: 26949248 pmcid: 4859805
Pierce, N. W. et al. Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins. Cell 153, 206–215 (2013).
pubmed: 23453757 pmcid: 3656483
Reitsma, J. M. et al. Composition and regulation of the cellular repertoire of SCF ubiquitin ligases. Cell 171, 1326–1339 (2017).
pubmed: 29103612 pmcid: 5711595
Liu, X. et al. Cand1-mediated adaptive exchange mechanism enables variation in F-box protein expression. Mol. Cell 69, 773–786 (2018).
pubmed: 29499133 pmcid: 5836512
Wu, S. et al. CAND1 controls in vivo dynamics of the cullin 1–RING ubiquitin ligase repertoire. Nat. Commun. 4, 1642 (2013).
pubmed: 23535663
Zemla, A. et al. CSN- and CAND1-dependent remodelling of the budding yeast SCF complex. Nat. Commun. 4, 1641 (2013).
pubmed: 23535662
Duda, D. M. et al. Structural insights into NEDD8 activation of cullin–RING ligases: conformational control of conjugation. Cell 134, 995–1006 (2008).
pubmed: 18805092 pmcid: 2628631
Kabsch, W. Xds. Acta Crystallogr. D 66, 125–132 (2010).
pubmed: 20124692 pmcid: 2815665
Evans, P. R. & Murshudov, G. N. How good are my data and what is the resolution? Acta Crystallogr. D 69, 1204–1214 (2013).
pubmed: 23793146 pmcid: 3689523
Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235–242 (2011).
pubmed: 21460441 pmcid: 3069738
Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213–221 (2010).
pubmed: 20124702 pmcid: 2815670
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486–501 (2010).
pubmed: 20383002 pmcid: 2852313
DiMaio, F. et al. Improved low-resolution crystallographic refinement with Phenix and Rosetta. Nat. Methods 10, 1102–1104 (2013).
pubmed: 24076763 pmcid: 4116791
Morin, A. et al. Collaboration gets the most out of software. eLife 2, e01456 (2013).
pubmed: 24040512 pmcid: 3771563
Grimsley, G. R., Huyghues-Despointes, B. M., Pace, C. N. & Scholtz, J. M. Preparation of urea and guanidinium chloride stock solutions for measuring denaturant-induced unfolding curves. CSH Protoc. 2006, pdb.prot4241 (2006).
pubmed: 22485638
McDonald, S. K. & Fleming, K. G. Aromatic side chain water-to-lipid transfer free energies show a depth dependence across the membrane normal. J. Am. Chem. Soc. 138, 7946–7950 (2016).
pubmed: 27254476 pmcid: 4927395
Tivol, W. F., Briegel, A. & Jensen, G. J. An improved cryogen for plunge freezing. Microsc. Microanal. 14, 375–379 (2008).
pubmed: 18793481 pmcid: 3058946
Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36–51 (2005).
pubmed: 16182563
Schorb, M., Haberbosch, I., Hagen, W. J. H., Schwab, Y. & Mastronarde, D. N. Software tools for automated transmission electron microscopy. Nat. Methods 16, 471–477 (2019).
pubmed: 31086343 pmcid: 7000238
Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331–332 (2017).
pubmed: 28250466 pmcid: 5494038
Biyani, N. et al. Focus: The interface between data collection and data processing in cryo-EM. J. Struct. Biol. 198, 124–133 (2017).
pubmed: 28344036
Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. eLife 7, e42166 (2018).
pubmed: 30412051 pmcid: 6250425
Zhang, K. Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193, 1–12 (2016).
pubmed: 26592709 pmcid: 4711343
Rohou, A. & Grigorieff, N. CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216–221 (2015).
pubmed: 26278980 pmcid: 6760662
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017).
pubmed: 28165473
Scheres, S. H. W. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nat. Methods 9, 853–854 (2012).
pubmed: 22842542 pmcid: 4912033
Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).
pubmed: 15264254
Afonine, P. V. et al. Real-space refinement in PHENIX for cryo-EM and crystallography. Acta Crystallogr. D 74, 531–544 (2018).
Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721–745 (2003).
pubmed: 14568533

Auteurs

Elijah L Mena (EL)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA.
Department of Genetics, Harvard Medical School, Boston, MA, USA.
ORCID: 0000-0001-9980-9018

Predrag Jevtić (P)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA.
Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA.

Basil J Greber (BJ)

California Institute for Quantitative Biosciences (QB3), University of California at Berkeley, Berkeley, CA, USA.
Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
ORCID: 0000-0001-9379-7159

Christine L Gee (CL)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA.
Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA.
ORCID: 0000-0002-2632-6418

Brandon G Lew (BG)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA.
Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA.

David Akopian (D)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA.

Eva Nogales (E)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA.
Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA.
California Institute for Quantitative Biosciences (QB3), University of California at Berkeley, Berkeley, CA, USA.
Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
ORCID: 0000-0001-9816-3681

John Kuriyan (J)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA.
Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA.
California Institute for Quantitative Biosciences (QB3), University of California at Berkeley, Berkeley, CA, USA.
Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Department of Chemistry, University of California at Berkeley, Berkeley, CA, USA.

Michael Rape (M)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA. mrape@berkeley.edu.
Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA. mrape@berkeley.edu.
California Institute for Quantitative Biosciences (QB3), University of California at Berkeley, Berkeley, CA, USA. mrape@berkeley.edu.
ORCID: 0000-0003-4849-6343

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Classifications MeSH

questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Éléments structuraux des protéines › Motifs et domaines d'intéraction protéique › Domaine BTB-POZ › Structural basis for dimerization quality control.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › Protéines F-box › Structural basis for dimerization quality control.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Structural basis for dimerization quality control.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines adaptatrices de la transduction du signal › Protéine-1 de type kelch associée à ECH › Structural basis for dimerization quality control.
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles biologiques › Structural basis for dimerization quality control.
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Structural basis for dimerization quality control.
questionsmedicales.fr › Métabolisme › Liaison aux protéines › Structural basis for dimerization quality control.
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Pliage des protéines › Structural basis for dimerization quality control.
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Multimérisation de protéines › Structural basis for dimerization quality control.
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Stabilité protéique › Structural basis for dimerization quality control.
questionsmedicales.fr › Facteurs biologiques › Protéines et peptides de signalisation intercellulaire › Cytokines › Facteurs de croissance hématopoïétique › Facteur de croissance des cellules souches › Structural basis for dimerization quality control.
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Ubiquitination › Structural basis for dimerization quality control.