Molecular basis of MKLP2-dependent Aurora B transport from chromatin to the anaphase central spindle

The Aurora B chromosomal passenger complex (CPC) is a conserved regulator of mitosis. Its functions require localization first to the chromosome arms and then centromeres in mitosis and subsequently the central spindle in anaphase. Here, we analyze the requirements for core CPC subunits, survivin an...

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Vydané v:The Journal of cell biology Ročník 219; číslo 7
Hlavní autori: Serena, Michela, Bastos, Ricardo Nunes, Elliott, Paul R, Barr, Francis A
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 06.07.2020
Predmet:
Amino Acid Sequence
Anaphase
Animals
Aurora Kinase B - chemistry
Aurora Kinase B - genetics
Aurora Kinase B - metabolism
Binding, Competitive
Centromere - metabolism
Centromere - ultrastructure
Chromatin - metabolism
Chromatin - ultrastructure
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - metabolism
DNA - chemistry
DNA - genetics
DNA - metabolism
HeLa Cells
Histones - chemistry
Histones - genetics
Histones - metabolism
Humans
Kinesins - chemistry
Kinesins - genetics
Kinesins - metabolism
Metaphase
Microtubules - metabolism
Microtubules - ultrastructure
Models, Molecular
Phosphorylation
Protein Binding
Protein Processing, Post-Translational
Protein Structure, Secondary
Protein Transport
Sequence Alignment
Sequence Homology, Amino Acid
Spindle Apparatus - metabolism
Spindle Apparatus - ultrastructure
Survivin - chemistry
Survivin - genetics
Survivin - metabolism
ISSN:1540-8140, 1540-8140
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Popis
Shrnutí:The Aurora B chromosomal passenger complex (CPC) is a conserved regulator of mitosis. Its functions require localization first to the chromosome arms and then centromeres in mitosis and subsequently the central spindle in anaphase. Here, we analyze the requirements for core CPC subunits, survivin and INCENP, and the mitotic kinesin-like protein 2 (MKLP2) in targeting to these distinct localizations. Centromere recruitment of the CPC requires interaction of survivin with histone H3 phosphorylated at threonine 3, and we provide a complete structure of this assembly. Furthermore, we show that the INCENP RRKKRR-motif is required for both centromeric localization of the CPC in metaphase and MKLP2-dependent transport in anaphase. MKLP2 and DNA bind competitively to this motif, and INCENP T59 phosphorylation acts as a switch preventing MKLP2 binding in metaphase. In anaphase, CPC binding promotes the microtubule-dependent ATPase activity of MKLP2. These results explain how centromere targeting of the CPC in mitosis is coupled to its movement to the central spindle in anaphase.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1540-8140
1540-8140
DOI:10.1083/jcb.201910059