148:, the majority of Mi2 biochemically purifies separately from the rest of the NuRD subunits and profiling of NuRD component binding sites indicates that only a minority of loci are co-occupied by both Mi-2 and HDAC. Similar results are reported in mouse embryonic stem cells where CHD4 shares only a minority of binding loci with core NuRD component, MBD3. Independently of histone deacetylase, Mi-2 knockdown in neuronal tissue results in mis-expression of genes that are normally restricted to germline. A similar observation was made in human erythroid cells, in which CHD4 but not Mi-2 is required for suppression of fetal globin genes.
285:
156:
NuRD is traditionally thought of as a primarily repressive complex, and in some contexts it is clear that it does confer this function. For example, NuRD is required to silence genes in neuronal differentiation. However, more recent studies have presented a more nuanced picture of NuRD activity in
127:
NuRD can be subdivided into two discrete subcomplexes which confer neuclosome remodelling or histone deacetylation activity,each of which retains catalytic activity without the presence of the other. The histone deacetylases
51:
In 1998, several independent groups reported the discovery of multi-enzyme complexes conferring both nucleosome remodelling and histone deacetylation activities. Xue et al first described the human complex as the
43:
activities. As of 2007, Mi-2/NuRD was the only known protein complex that couples chromatin remodeling ATPase and chromatin deacetylation enzymatic functions.
298:
Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (October 1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex".
734:"The Nucleosome Remodeling and Deacetylation Complex Modulates Chromatin Structure at Sites of Active Transcription to Fine-Tune Gene Expression"
548:"The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities"
417:"The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities"
157:
which it is required for fine-tuning of gene expression during stem cell differentiation to ensure appropriate lineage specification.
136:
and the histone binding proteins RbAp48 and RbAp46 form a core complex shared between NuRD and Sin3-histone deacetylase complexes.
335:"A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase"
144:
Mi-2/CHD4 may confer NuRD independent transcriptional regulation in some organisms and contexts. For example, in the fly,
832:"Promoter decommissioning by the NuRD chromatin remodeling complex triggers synaptic connectivity in the mammalian brain"
884:
450:"The Nucleosome Remodeling and Deacetylase Complex NuRD Is Built from Preformed Catalytically Active Sub-modules"
499:"Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation"
284:
32:
133:
376:"NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities"
178:"NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities"
77:
36:
40:
448:
Zhang W, Aubert A, Gomez de Segura JM, Karuppasamy M, Basu S, Murthy AS, et al. (July 2016).
732:
Bornelöv S, Reynolds N, Xenophontos M, Gharbi S, Johnstone E, Floyd R, et al. (July 2018).
861:
812:
763:
711:
659:
610:
569:
528:
479:
397:
356:
315:
273:
199:
20:
682:"NuRD-independent Mi-2 activity represses ectopic gene expression during neuronal maturation"
851:
843:
802:
794:
781:
Amaya M, Desai M, Gnanapragasam MN, Wang SZ, Zu Zhu S, Williams DC, Ginder GD (April 2013).
753:
745:
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641:
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559:
518:
510:
469:
461:
428:
387:
346:
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230:
189:
630:"dMec: a novel Mi-2 chromatin remodelling complex involved in transcriptional repression"
706:
681:
856:
831:
807:
782:
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733:
654:
629:
474:
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547:
523:
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177:
878:
830:
Yamada T, Yang Y, Hemberg M, Yoshida T, Cho HY, Murphy JP, et al. (July 2014).
847:
798:
749:
497:
Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (August 1999).
68:) - this name has since been adopted for homologous complexes in most organisms.
465:
783:"Mi2β-mediated silencing of the fetal γ-globin gene in adult erythroid cells"
697:
628:
Kunert N, Wagner E, Murawska M, Klinker H, Kremmer E, Brehm A (March 2009).
865:
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532:
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277:
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573:
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645:
235:
218:
605:
588:
93:
680:
Aughey GN, Forsberg E, Grimes K, Zhang S, Southall TD (April 2023).
374:
Xue Y, Wong J, Moreno GT, Young MK, Côté J, Wang W (December 1998).
176:
Xue Y, Wong J, Moreno GT, Young MK, Côté J, Wang W (December 1998).
311:
129:
89:
85:
81:
546:
Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (October 1998).
415:
Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (October 1998).
121:
117:
113:
109:
105:
101:
97:
80:
contains seven subunits: the histone deacetylase core proteins
589:"Novel Mi-2 related ATP-dependent chromatin remodelers"
219:"The Expanding Mi-2/NuRD Complexes: A Schematic Glance"
333:
Wade PA, Jones PL, Vermaak D, Wolffe AP (July 1998).
727:
725:
116:) and the chromodomain-helicase-DNA-binding protein
252:"The human Mi-2/NuRD complex and gene regulation"
31:, is a group of associated proteins with both
171:
169:
8:
855:
806:
757:
705:
653:
604:
563:
522:
473:
432:
391:
350:
267:
234:
193:
108:), the methyl-CpG-binding domain protein
165:
675:
673:
96:, the metastasis-associated proteins
7:
27:(Nucleosome Remodeling Deacetylase)
250:Denslow SA, Wade PA (August 2007).
140:NuRD-independent Mi2/CHD4 activity
14:
283:
88:, the histone-binding proteins
587:Kunert N, Brehm A (May 2009).
1:
565:10.1016/S0092-8674(00)81758-4
434:10.1016/S0092-8674(00)81758-4
393:10.1016/S1097-2765(00)80299-3
352:10.1016/S0960-9822(98)70328-8
195:10.1016/S1097-2765(00)80299-3
848:10.1016/j.neuron.2014.05.039
799:10.1182/blood-2012-11-466227
750:10.1016/j.molcel.2018.06.003
454:Journal of Molecular Biology
152:Biological functions of NuRD
217:Zhang Y, Yinghua L (2010).
901:
466:10.1016/j.jmb.2016.04.025
698:10.15252/embr.202255362
503:Genes & Development
146:Drosophila melanogaster
515:10.1101/gad.13.15.1924
269:10.1038/sj.onc.1210611
646:10.1038/emboj.2009.3
37:chromatin remodeling
223:Proteomics Insights
120:(aka Mi-2alpha) or
41:histone deacetylase
885:Protein complexes
793:(17): 3493–3501.
509:(15): 1924–1935.
460:(14): 2931–2942.
306:(6705): 917–921.
262:(37): 5433–5438.
236:10.4137/PRI.S6329
21:molecular biology
892:
870:
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634:The EMBO Journal
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124:(aka Mi-2beta).
19:In the field of
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744:(1): 56–72.e4.
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345:(14): 843–846.
339:Current Biology
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60:emodelling and
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17:
16:Protein complex
12:
11:
5:
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872:
871:
842:(1): 122–134.
822:
773:
738:Molecular Cell
721:
669:
640:(5): 533–544.
620:
599:(4): 209–211.
579:
558:(2): 279–289.
538:
489:
440:
427:(2): 279–289.
407:
386:(6): 851–861.
380:Molecular Cell
366:
325:
290:
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188:(6): 851–861.
182:Molecular Cell
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692:(4): e55362.
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686:EMBO Reports
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65:
64:eacetylase (
61:
57:
53:
50:
28:
24:
18:
593:Epigenetics
72:Composition
35:-dependent
229:: 79–109.
161:References
76:The NuRD
56:cleosome
47:Discovery
25:Mi-2/NuRD
879:Category
866:24991957
817:23444401
768:30008319
716:36722816
707:10074086
664:19165147
615:19535903
533:10444591
484:27117189
278:17694084
256:Oncogene
857:4266462
808:3637018
759:6039721
655:2657585
574:9790534
475:4942838
402:9885572
361:9663395
320:9804427
204:9885572
78:complex
29:complex
864:
854:
836:Neuron
815:
805:
766:
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714:
704:
662:
652:
613:
572:
531:
524:316920
521:
482:
472:
400:
359:
318:
300:Nature
276:
202:
94:RbAp48
90:RbAp46
23:, the
787:Blood
134:HDAC2
130:HDAC1
86:HDAC2
82:HDAC1
862:PMID
813:PMID
764:PMID
712:PMID
660:PMID
611:PMID
570:PMID
552:Cell
529:PMID
480:PMID
421:Cell
398:PMID
357:PMID
316:PMID
274:PMID
200:PMID
132:and
122:CHD4
118:CHD3
114:MBD2
112:(or
110:MBD3
106:MTA3
102:MTA2
100:(or
98:MTA1
92:and
84:and
66:NuRD
39:and
852:PMC
844:doi
803:PMC
795:doi
791:121
754:PMC
746:doi
702:PMC
694:doi
650:PMC
642:doi
601:doi
560:doi
519:PMC
511:doi
470:PMC
462:doi
458:428
429:doi
388:doi
347:doi
308:doi
304:395
264:doi
231:doi
190:doi
33:ATP
881::
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850:.
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838:.
834:.
811:.
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789:.
785:.
762:.
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742:71
740:.
736:.
724:^
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690:24
688:.
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672:^
658:.
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260:26
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168:^
104:/
54:Nu
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233::
227:3
206:.
192::
186:2
62:D
58:R
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