Molecular architecture of a cylindrical self-assembly at human centrosomes.
Amino Acid Motifs
/ genetics
Cell Cycle Proteins
/ chemistry
Cell Line, Tumor
Centrioles
/ metabolism
Crystallography, X-Ray
HEK293 Cells
Humans
Hydrophobic and Hydrophilic Interactions
Microscopy, Fluorescence
Mutation
Neoplasm Proteins
/ chemistry
Protein Conformation, alpha-Helical
Protein Multimerization
/ physiology
Protein Serine-Threonine Kinases
/ isolation & purification
RNA, Small Interfering
/ metabolism
Recombinant Proteins
/ genetics
Time-Lapse Imaging
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
11 03 2019
11 03 2019
Historique:
received:
23
05
2018
accepted:
01
02
2019
entrez:
13
3
2019
pubmed:
13
3
2019
medline:
6
4
2019
Statut:
epublish
Résumé
The cell is constructed by higher-order structures and organelles through complex interactions among distinct structural constituents. The centrosome is a membraneless organelle composed of two microtubule-derived structures called centrioles and an amorphous mass of pericentriolar material. Super-resolution microscopic analyses in various organisms revealed that diverse pericentriolar material proteins are concentrically localized around a centriole in a highly organized manner. However, the molecular nature underlying these organizations remains unknown. Here we show that two human pericentriolar material scaffolds, Cep63 and Cep152, cooperatively generate a heterotetrameric α-helical bundle that functions in conjunction with its neighboring hydrophobic motifs to self-assemble into a higher-order cylindrical architecture capable of recruiting downstream components, including Plk4, a key regulator for centriole duplication. Mutations disrupting the self-assembly abrogate Plk4-mediated centriole duplication. Because pericentriolar material organization is evolutionarily conserved, this work may offer a paradigm for investigating the assembly and function of centrosomal scaffolds in various organisms.
Identifiants
pubmed: 30858376
doi: 10.1038/s41467-019-08838-2
pii: 10.1038/s41467-019-08838-2
pmc: PMC6411776
doi:
Substances chimiques
CEP152 protein, human
0
CEP63 protein, human
0
Cell Cycle Proteins
0
Neoplasm Proteins
0
RNA, Small Interfering
0
Recombinant Proteins
0
PLK4 protein, human
EC 2.7.1.-
Protein Serine-Threonine Kinases
EC 2.7.11.1
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Research Support, Non-U.S. Gov't
Video-Audio Media
Langues
eng
Sous-ensembles de citation
IM
Pagination
1151Références
J Cell Biol. 2011 Oct 17;195(2):231-43
pubmed: 21987638
Nat Rev Cancer. 2015 Nov;15(11):639-52
pubmed: 26493645
Nat Struct Mol Biol. 2014 Aug;21(8):696-703
pubmed: 24997597
Nat Commun. 2014 Oct 24;5:5267
pubmed: 25342035
J Cell Biol. 2014 Mar 3;204(5):697-712
pubmed: 24590172
EMBO J. 2011 Oct 21;30(23):4790-804
pubmed: 22020124
Chem Rev. 2008 Apr;108(4):1225-44
pubmed: 18355092
J Cell Sci. 2013 Jul 15;126(Pt 14):3223-33
pubmed: 23641073
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
J Cell Sci. 2007 Dec 15;120(Pt 24):4247-60
pubmed: 18057027
Biol Open. 2012 Oct 15;1(10):965-76
pubmed: 23213374
Science. 1991 May 24;252(5009):1162-4
pubmed: 2031185
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42
pubmed: 21460441
Trends Biochem Sci. 2017 Feb;42(2):130-140
pubmed: 27884598
Cell. 2011 Feb 4;144(3):364-75
pubmed: 21277013
Biophys J. 2000 Mar;78(3):1606-19
pubmed: 10692345
Cold Spring Harb Perspect Biol. 2015 Feb 02;7(2):a015800
pubmed: 25646378
Nat Cell Biol. 2013 Dec;15(12):1434-44
pubmed: 24240477
Science. 2009 Mar 6;323(5919):1354-7
pubmed: 19265022
J Cell Biol. 2010 Nov 15;191(4):721-9
pubmed: 21059850
Cell. 2003 Oct 3;115(1):83-95
pubmed: 14532005
Mol Cell Biol. 1995 Dec;15(12):7143-51
pubmed: 8524282
Mol Biol Cell. 2012 Jun;23(11):2198-212
pubmed: 22496416
Methods Enzymol. 1997;276:307-26
pubmed: 27754618
PLoS One. 2013 Jul 17;8(7):e69004
pubmed: 23874848
Biochem Soc Trans. 2016 Oct 15;44(5):1253-1263
pubmed: 27911707
Nat Cell Biol. 2012 Nov;14(11):1148-58
pubmed: 23086237
Science. 2009 Aug 21;325(5943):960-3
pubmed: 19696342
Cell. 2017 Jun 1;169(6):1078-1089.e13
pubmed: 28575671
J Cell Sci. 2012 Mar 1;125(Pt 5):1342-52
pubmed: 22349698
Mol Cell Biol. 1987 Aug;7(8):2745-52
pubmed: 3670292
Biol Open. 2015 Feb 20;4(3):370-7
pubmed: 25701666
Nat Rev Mol Cell Biol. 2014 Jul;15(7):433-52
pubmed: 24954208
Curr Biol. 2014 Jun 2;24(11):1276-82
pubmed: 24835456
Nat Cell Biol. 2012 Nov;14(11):1159-68
pubmed: 23086239
Annu Rev Cell Dev Biol. 2017 Oct 6;33:23-49
pubmed: 28813178
J Cell Biol. 2010 Nov 15;191(4):731-9
pubmed: 21059844
J Cell Sci. 2012 Mar 1;125(Pt 5):1353-62
pubmed: 22349705
Cold Spring Harb Perspect Biol. 2016 Dec 1;8(12):
pubmed: 27908937
Nat Genet. 2011 Oct 09;43(11):1147-53
pubmed: 21983783
Cell. 2017 Jun 1;169(6):1066-1077.e10
pubmed: 28575670
Proc Natl Acad Sci U S A. 2013 Dec 10;110(50):E4849-57
pubmed: 24277814
Curr Protoc Protein Sci. 2013 Feb;Chapter 20:Unit20.12
pubmed: 23377850
Nat Rev Mol Cell Biol. 2015 Oct;16(10):611-24
pubmed: 26373263
Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67
pubmed: 22505256
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
pubmed: 15572765
Open Biol. 2012 Aug;2(8):120104
pubmed: 22977736
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21
pubmed: 20124702
Methods Cell Biol. 2008;84:143-79
pubmed: 17964931
Nat Commun. 2015 Jul 09;6:7676
pubmed: 26158450
Nature. 2005 Sep 29;437(7059):640-7
pubmed: 16193038
PLoS One. 2013 Jul 30;8(7):e69986
pubmed: 23936128
Curr Biol. 2013 Feb 4;23(3):265-70
pubmed: 23333316
Science. 2015 May 15;348(6236):808-12
pubmed: 25977552
J Cell Biol. 2015 Jun 22;209(6):863-78
pubmed: 26101219
Nat Rev Mol Cell Biol. 2018 May;19(5):297-312
pubmed: 29363672
Nat Genet. 2011 Jan;43(1):23-6
pubmed: 21131973
Elife. 2015 Aug 22;4:
pubmed: 26297806