Calcium modulates the tethering of BCOR-PRC1.1 enzymatic core to KDM2B via liquid-liquid phase separation.

Proto-Oncogene Proteins / metabolism Repressor Proteins / metabolism Calcium / metabolism Humans Jumonji Domain-Containing Histone Demethylases / metabolism Polycomb Repressive Complex 1 / metabolism Protein Binding Phase Separation F-Box Proteins

Journal

Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179

Informations de publication

Date de publication:
10 Sep 2024
Historique:
received: 23 01 2024
accepted: 31 08 2024
medline: 11 9 2024
pubmed: 11 9 2024
entrez: 10 9 2024
Statut: epublish

Résumé

Recruitment of non-canonical BCOR-PRC1.1 to non-methylated CpG islands via KDM2B plays a fundamental role in transcription control during developmental processes and cancer progression. However, the mechanism is still largely unknown on how this recruitment is regulated. Here, we unveiled the importance of the Poly-D/E regions within the linker of BCOR for its binding to KDM2B. Interestingly, we also demonstrated that these negatively charged Poly-D/E regions on BCOR play autoinhibitory roles in liquid-liquid phase separation (LLPS) of BCOR

Identifiants

DOI: 10.1038/s42003-024-06820-3 PMID: 39256555
pubmed: 39256555
doi: 10.1038/s42003-024-06820-3
pii: 10.1038/s42003-024-06820-3
doi:

Substances chimiques

Proto-Oncogene Proteins 0
Repressor Proteins 0
Calcium SY7Q814VUP
Jumonji Domain-Containing Histone Demethylases EC 1.14.11.-
Polycomb Repressive Complex 1 EC 2.3.2.27
BCOR protein, human 0
KDM2A protein, human EC 1.14.11.27
F-Box Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

1112

Informations de copyright

© 2024. The Author(s).

Références

Jaenisch, R. & Bird, A. Epigenetic regulation of gene expression: how the genome integrates intrinsic and environmental signals. Nat. Genet. 33, 245–254 (2003).
pubmed: 12610534 doi: 10.1038/ng1089
Kouzarides, T. Chromatin modifications and their function. Cell 128, 693–705 (2007).
pubmed: 17320507 doi: 10.1016/j.cell.2007.02.005
Blackledge, N. P. & Klose, R. J. The molecular principles of gene regulation by polycomb repressive complexes. Nat. Rev. Mol. Cell Biol. 22, 815–833 (2021).
pubmed: 34400841 pmcid: 7612013 doi: 10.1038/s41580-021-00398-y
Jaenisch, R. & Young, R. Stem cells, the molecular circuitry of pluripotency and nuclear reprogramming. Cell 132, 567–582 (2008).
pubmed: 18295576 pmcid: 4142810 doi: 10.1016/j.cell.2008.01.015
Margueron, R. & Reinberg, D. The polycomb complex PRC2 and its mark in life. Nature 469, 343–349 (2011).
pubmed: 21248841 pmcid: 3760771 doi: 10.1038/nature09784
Sparmann, A. & van Lohuizen, M. Polycomb silencers control cell fate, development and cancer. Nat. Rev. Cancer 6, 846–856 (2006).
pubmed: 17060944 doi: 10.1038/nrc1991
Schuettengruber, B., Bourbon, H. M., Di Croce, L. & Cavalli, G. Genome regulation by polycomb and trithorax: 70 years and counting. Cell 171, 34–57 (2017).
pubmed: 28938122 doi: 10.1016/j.cell.2017.08.002
Simon, J. A. & Kingston, R. E. Occupying chromatin: polycomb mechanisms for getting to genomic targets, stopping transcriptional traffic, and staying put. Mol. Cell 49, 808–824 (2013).
pubmed: 23473600 pmcid: 3628831 doi: 10.1016/j.molcel.2013.02.013
Barbour, H., Daou, S., Hendzel, M. & Affar, E. B. Polycomb group-mediated histone H2A monoubiquitination in epigenome regulation and nuclear processes. Nat. Commun. 11, 5947 (2020).
pubmed: 33230107 pmcid: 7683540 doi: 10.1038/s41467-020-19722-9
Hojfeldt, J. W. et al. Accurate H3K27 methylation can be established de novo by SUZ12-directed PRC2. Nat. Struct. Mol. Biol. 25, 225–232 (2018).
pubmed: 29483650 pmcid: 5842896 doi: 10.1038/s41594-018-0036-6
Margueron, R. et al. Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol. Cell 32, 503–518 (2008).
pubmed: 19026781 pmcid: 3641558 doi: 10.1016/j.molcel.2008.11.004
Chittock, E. C., Latwiel, S., Miller, T. C. & Muller, C. W. Molecular architecture of polycomb repressive complexes. Biochem. Soc. Trans. 45, 193–205 (2017).
pubmed: 28202673 pmcid: 5310723 doi: 10.1042/BST20160173
Gao, Z. et al. PCGF homologs, CBX proteins, and RYBP define functionally distinct PRC1 family complexes. Mol. Cell 45, 344–356 (2012).
pubmed: 22325352 pmcid: 3293217 doi: 10.1016/j.molcel.2012.01.002
Aranda, S., Mas, G. & Di Croce, L. Regulation of gene transcription by polycomb proteins. Sci. Adv. 1, e1500737 (2015).
pubmed: 26665172 pmcid: 4672759 doi: 10.1126/sciadv.1500737
Gil, J. & O’Loghlen, A. PRC1 complex diversity: where is it taking us? Trends Cell Biol. 24, 632–641 (2014).
pubmed: 25065329 doi: 10.1016/j.tcb.2014.06.005
Fursova, N. A. et al. Synergy between variant PRC1 complexes defines polycomb-mediated gene repression. Mol. Cell 74, 1020–1036 e8 (2019).
pubmed: 31029541 pmcid: 6561741 doi: 10.1016/j.molcel.2019.03.024
Taherbhoy, A. M., Huang, O. W. & Cochran, A. G. BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase. Nat. Commun. 6, 7621 (2015).
pubmed: 26151332 doi: 10.1038/ncomms8621
Zhu, Y. et al. Functional redundancy among polycomb complexes in maintaining the pluripotent state of embryonic stem cells. Stem. Cell Rep. 17, 1198–1214 (2022).
doi: 10.1016/j.stemcr.2022.02.020
Aldera, A. P. & Govender, D. Gene of the month: BCOR. J. Clin. Pathol. 73, 314–317 (2020).
pubmed: 32161069 doi: 10.1136/jclinpath-2020-206513
He, J. et al. Kdm2b maintains murine embryonic stem cell status by recruiting PRC1 complex to CpG islands of developmental genes. Nat. Cell Biol. 15, 373–384 (2013).
pubmed: 23502314 pmcid: 4078788 doi: 10.1038/ncb2702
Isshiki, Y. et al. KDM2B in polycomb repressive complex 1.1 functions as a tumor suppressor in the initiation of T-cell leukemogenesis. Blood Adv. 3, 2537–2549 (2019).
pubmed: 31471323 pmcid: 6737409 doi: 10.1182/bloodadvances.2018028522
Wang, Z. et al. A non-canonical BCOR-PRC1.1 complex represses differentiation programs in human ESCs. Cell Stem. Cell 22, 235–251 e9 (2018).
pubmed: 29337181 pmcid: 5797497 doi: 10.1016/j.stem.2017.12.002
Tiacci, E. et al. The corepressors BCOR and BCORL1: two novel players in acute myeloid leukemia. Haematologica 97, 3–5 (2012).
pubmed: 22210327 pmcid: 3248923 doi: 10.3324/haematol.2011.057901
van den Boom, V. et al. Non-canonical PRC1.1 targets active genes independent of H3K27me3 and is essential for leukemogenesis. Cell Rep 14, 332–346 (2016).
pubmed: 26748712 doi: 10.1016/j.celrep.2015.12.034
Lempiainen, J. K. et al. BCOR-coupled H2A monoubiquitination represses a subset of androgen receptor target genes regulating prostate cancer proliferation. Oncogene 39, 2391–2407 (2020).
pubmed: 31925334 doi: 10.1038/s41388-020-1153-3
Deaton, A. M. & Bird, A. CpG islands and the regulation of transcription. Genes Dev. 25, 1010–1022 (2011).
pubmed: 21576262 pmcid: 3093116 doi: 10.1101/gad.2037511
Farcas, A. M. et al. KDM2B links the Polycomb Repressive Complex 1 (PRC1) to recognition of CpG islands. Elife 1, e00205 (2012).
pubmed: 23256043 pmcid: 3524939 doi: 10.7554/eLife.00205
Wu, X., Johansen, J. V. & Helin, K. Fbxl10/Kdm2b recruits polycomb repressive complex 1 to CpG islands and regulates H2A ubiquitylation. Mol. Cell 49, 1134–1146 (2013).
pubmed: 23395003 doi: 10.1016/j.molcel.2013.01.016
Xie, W. et al. Epigenomic analysis of multilineage differentiation of human embryonic stem cells. Cell 153, 1134–1148 (2013).
pubmed: 23664764 pmcid: 3786220 doi: 10.1016/j.cell.2013.04.022
Saxonov, S., Berg, P. & Brutlag, D. L. A genome-wide analysis of CpG dinucleotides in the human genome distinguishes two distinct classes of promoters. Proc. Natl Acad. Sci. USA 103, 1412–1417 (2006).
pubmed: 16432200 pmcid: 1345710 doi: 10.1073/pnas.0510310103
Schaefer, E. J. et al. BCOR and BCORL1 mutations drive epigenetic reprogramming and oncogenic signaling by unlinking PRC1.1 from target genes. Blood Cancer Discov. 3, 116–135 (2022).
pubmed: 35015684 pmcid: 9414116 doi: 10.1158/2643-3230.BCD-21-0115
Wong, S. J. et al. KDM2B recruitment of the polycomb group complex, PRC1.1, requires cooperation between PCGF1 and BCORL1. Structure 24, 1795–1801 (2016).
pubmed: 27568929 pmcid: 5088048 doi: 10.1016/j.str.2016.07.011
Wong, S. J. et al. Structure and role of BCOR PUFD in noncanonical PRC1 assembly and disease. Biochemistry 59, 2718–2728 (2020).
pubmed: 32628469 doi: 10.1021/acs.biochem.0c00285
Boulard, M., Edwards, J. R. & Bestor, T. H. FBXL10 protects polycomb-bound genes from hypermethylation. Nat. Genet. 47, 479–485 (2015).
pubmed: 25848754 doi: 10.1038/ng.3272
Sportoletti, P., Sorcini, D. & Falini, B. BCOR gene alterations in hematologic diseases. Blood 138, 2455–2468 (2021).
pubmed: 33945606 pmcid: 8887995 doi: 10.1182/blood.2021010958
de Miranda, M. C. et al. Epidermal growth factor (EGF) triggers nuclear calcium signaling through the intranuclear phospholipase Cdelta-4 (PLCdelta4). J. Biol. Chem. 294, 16650–16662 (2019).
pubmed: 31537645 pmcid: 6851314 doi: 10.1074/jbc.RA118.006961
Alonso, M. T. & Garcia-Sancho, J. Nuclear Ca(2+) signalling. Cell Calcium 49, 280–289 (2011).
pubmed: 21146212 doi: 10.1016/j.ceca.2010.11.004
Kunrath-Lima, M. et al. Phospholipase C delta 4 (PLCdelta4) is a nuclear protein involved in cell proliferation and senescence in mesenchymal stromal stem cells. Cell Signal 49, 59–67 (2018).
pubmed: 29859928 pmcid: 6095203 doi: 10.1016/j.cellsig.2018.05.011
Chun, J.T., Santella, L. & Miller, J.J. Calcium | intracellular calcium waves. In Encyclopedia of Biological Chemistry III (ed. Jez, J.) 669–677 (Elsevier, 2021).
Vernon, R.M. et al. Pi-Pi contacts are an overlooked protein feature relevant to phase separation. Elife 7, e31486 (2018).
Nakajima-Takagi, Y. et al. Polycomb repressive complex 1.1 coordinates homeostatic and emergency myelopoiesis. eLife 12, e83004 (2023).
Sato, K., Fukami, Y. & Stith, B. J. Signal transduction pathways leading to Ca2+ release in a vertebrate model system: lessons from Xenopus eggs. Semin Cell Dev. Biol. 17, 285–292 (2006).
pubmed: 16584903 doi: 10.1016/j.semcdb.2006.02.008
Monteith, G. R., Prevarskaya, N. & Roberts-Thomson, S. J. The calcium-cancer signalling nexus. Nat. Rev. Cancer 17, 367–380 (2017).
pubmed: 28386091 doi: 10.1038/nrc.2017.18
So, C. L., Saunus, J. M., Roberts-Thomson, S. J. & Monteith, G. R. Calcium signalling and breast cancer. Semin. Cell Dev. Biol. 94, 74–83 (2019).
pubmed: 30439562 doi: 10.1016/j.semcdb.2018.11.001
Izquierdo-Torres, E., Hernandez-Oliveras, A., Fuentes-Garcia, G. & Zarain-Herzberg, A. Calcium signaling and epigenetics: a key point to understand carcinogenesis. Cell Calcium 91, 102285 (2020).
pubmed: 32942140 doi: 10.1016/j.ceca.2020.102285
Shi, X. et al. Ca2+ regulates T-cell receptor activation by modulating the charge property of lipids. Nature 493, 111–115 (2013).
pubmed: 23201688 doi: 10.1038/nature11699
Berridge, M. J., Bootman, M. D. & Roderick, H. L. Calcium signalling: dynamics, homeostasis and remodelling. Nat. Rev. Mol. Cell Biol. 4, 517–529 (2003).
pubmed: 12838335 doi: 10.1038/nrm1155
Snoeck, H. W. Calcium regulation of stem cells. EMBO Rep. 21, e50028 (2020).
pubmed: 32419314 pmcid: 7271657 doi: 10.15252/embr.202050028
Clapham, D. E. Calcium signaling. Cell 131, 1047–1058 (2007).
pubmed: 18083096 doi: 10.1016/j.cell.2007.11.028
Wang, L. et al. Histone modifications regulate chromatin compartmentalization by contributing to a phase separation mechanism. Mol. Cell 76, 646–659 e6 (2019).
pubmed: 31543422 doi: 10.1016/j.molcel.2019.08.019
Sanulli, S. et al. HP1 reshapes nucleosome core to promote phase separation of heterochromatin. Nature 575, 390–394 (2019).
pubmed: 31618757 pmcid: 7039410 doi: 10.1038/s41586-019-1669-2
Zhang, H. et al. Liquid-liquid phase separation in biology: mechanisms, physiological functions and human diseases. Sci. China Life Sci. 63, 953–985 (2020).
pubmed: 32548680 doi: 10.1007/s11427-020-1702-x
Pirrotta, V. & Li, H. B. A view of nuclear polycomb bodies. Curr. Opin. Genet. Dev. 22, 101–109 (2012).
pubmed: 22178420 doi: 10.1016/j.gde.2011.11.004
Eeftens, J. M., Kapoor, M. & Brangwynne, C. P. Epigenetic memory as a time integral over prior history of polycomb phase separation. bioRvix https://doi.org/10.1101/2020.08.19.254706 (2020).
Guo, Y., Zhao, S. & Wang, G. G. Polycomb gene silencing mechanisms: PRC2 chromatin targeting, H3K27me3 ‘readout’, and phase separation-based compaction. Trends Genet. 37, 547–565 (2021).
pubmed: 33494958 pmcid: 8119337 doi: 10.1016/j.tig.2020.12.006
Plys, A. J. et al. Phase separation of polycomb-repressive complex 1 is governed by a charged disordered region of CBX2. Genes Dev. 33, 799–813 (2019).
pubmed: 31171700 pmcid: 6601514 doi: 10.1101/gad.326488.119
Fox, C. H. et al. A method for measuring intracellular free magnesium concentration in platelets using flow cytometry. Magnes Res. 20, 200–207 (2007).
pubmed: 17972463
Maat, H. et al. The USP7-TRIM27 axis mediates non-canonical PRC1.1 function and is a druggable target in leukemia. iScience 24, 102435 (2021).
pubmed: 34113809 pmcid: 8169803 doi: 10.1016/j.isci.2021.102435
Zhang, W.-Z. et al. The protein complex crystallography beamline (BL19U1) at the shanghai synchrotron radiation facility. Nuclear Sci. Tech. 30, 170 (2019).
doi: 10.1007/s41365-019-0683-2
Evans, P. R. An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta. Crystallogr. D Biol. Crystallogr. 67, 282–292 (2011).
pubmed: 21460446 pmcid: 3069743 doi: 10.1107/S090744491003982X
Lebedev, A. A., Vagin, A. A. & Murshudov, G. N. Model preparation in MOLREP and examples of model improvement using X-ray data. Acta. Crystallogr. D Biol. Crystallogr. 64, 33–39 (2008).
pubmed: 18094465 doi: 10.1107/S0907444907049839
Kovalevskiy, O., Nicholls, R. A., Long, F., Carlon, A. & Murshudov, G. N. Overview of refinement procedures within REFMAC5: utilizing data from different sources. Acta. Crystallogr. D Struct. Biol. 74, 215–227 (2018).
pubmed: 29533229 pmcid: 5947762 doi: 10.1107/S2059798318000979
Yang, B. et al. Identification of cross-linked peptides from complex samples. Nat. Methods 9, 904–906 (2012).
pubmed: 22772728 doi: 10.1038/nmeth.2099
Lu, S. et al. Mapping native disulfide bonds at a proteome scale. Nat. Methods 12, 329–331 (2015).
pubmed: 25664544 doi: 10.1038/nmeth.3283
Schneidman-Duhovny, D., Hammel, M. & Sali, A. Macromolecular docking restrained by a small angle X-ray scattering profile. J. Struct. Biol. 173, 461–471 (2011).
pubmed: 20920583 doi: 10.1016/j.jsb.2010.09.023
Schneidman-Duhovny, D., Hammel, M., Tainer, J. A. & Sali, A. FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles. Nucleic Acids Res. 44, W424–W429 (2016).
pubmed: 27151198 pmcid: 4987932 doi: 10.1093/nar/gkw389
Fiser, A., Do, R. K. & Sali, A. Modeling of loops in protein structures. Protein Sci. 9, 1753–1773 (2000).
pubmed: 11045621 pmcid: 2144714 doi: 10.1110/ps.9.9.1753

Auteurs

Rui Chen (R)

Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, 230026, China.
State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.

Feng Shen (F)

Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, 230026, China.
State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.

Yulong Zhang (Y)

State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.

Mingze Sun (M)

State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
Guangdong Provincial Key Laboratory of Biocomputing, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
China-New Zealand Joint Laboratory on Biomedicine and Health, Guangzhou, 510530, China.

Yan Dong (Y)

State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
Guangdong Provincial Key Laboratory of Biocomputing, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
China-New Zealand Joint Laboratory on Biomedicine and Health, Guangzhou, 510530, China.

Yue Yin (Y)

National Facility for Protein Science in Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Science, Shanghai, 201210, China.
ORCID: 0000-0002-7693-3910

Chen Su (C)

National Facility for Protein Science in Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Science, Shanghai, 201210, China.

Chao Peng (C)

National Facility for Protein Science in Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Science, Shanghai, 201210, China.
ORCID: 0000-0002-6814-2676

Jinsong Liu (J)

Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, 230026, China. liu_jinsong@gibh.ac.cn.
State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China. liu_jinsong@gibh.ac.cn.
Guangdong Provincial Key Laboratory of Biocomputing, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China. liu_jinsong@gibh.ac.cn.
China-New Zealand Joint Laboratory on Biomedicine and Health, Guangzhou, 510530, China. liu_jinsong@gibh.ac.cn.
ORCID: 0000-0003-2317-0558

Jinxin Xu (J)

State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China. xu_jinxin@gibh.ac.cn.
Guangdong Provincial Key Laboratory of Biocomputing, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China. xu_jinxin@gibh.ac.cn.
China-New Zealand Joint Laboratory on Biomedicine and Health, Guangzhou, 510530, China. xu_jinxin@gibh.ac.cn.
Key Laboratory of Regenerative Biology, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China. xu_jinxin@gibh.ac.cn.
ORCID: 0000-0002-1680-7533

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Ciara Duggan, Adam L Beckman, Ishani Ganguli et al.
1.00
Humans United States Aged Cross-Sectional Studies Medicare Part C

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Hallie Tankha, Devyn Gaskins, Amanda Shallcross et al.
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines tumorales › Protéines oncogènes › Protéines proto-oncogènes › Calcium modulates the tethering of BCOR-PRC1.1...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Protéines de répression › Calcium modulates the tethering of BCOR-PRC1.1...
questionsmedicales.fr › Facteurs biologiques › Facteurs de la coagulation sanguine › Calcium › Calcium modulates the tethering of BCOR-PRC1.1...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Calcium modulates the tethering of BCOR-PRC1.1...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Oxidoreductases › Oxygénases › Dioxygenases › Jumonji Domain-Containing Histone Demethylases › Calcium modulates the tethering of BCOR-PRC1.1...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Protéines de répression › Protéines du groupe Polycomb › Complexe répresseur Polycomb-1 › Calcium modulates the tethering of BCOR-PRC1.1...
questionsmedicales.fr › Métabolisme › Liaison aux protéines › Calcium modulates the tethering of BCOR-PRC1.1...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › Protéines F-box › Calcium modulates the tethering of BCOR-PRC1.1...