Journal
MOLECULAR CELL
Volume 65, Issue 1, Pages 66-77Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2016.11.001
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Funding
- Wellcome Trust [098391/Z/12/7, 090944/Z/09/Z]
- Cancer Research UK [C434/A13067]
- BBSRC [BB/J015199/1]
- Marie Curie fellowship [297881]
- EU Initial Training Network (ITN) UPSTREAM'' [PITN-GA-2011-290257]
- ISSF - Wellcome Trust [105606/Z/14/Z]
- NIH Office of Research Infrastructure Programs [P40 OD010440]
- Wellcome Trust Technology Platform'' award [097945/B/11/Z]
- MRC Next Generation Optical Microscopy'' award [MR/K015869/1]
- Wellcome Trust award [101468/Z/13/Z]
- Biotechnology and Biological Sciences Research Council [BB/J015199/1] Funding Source: researchfish
- Cancer Research UK [21747] Funding Source: researchfish
- Wellcome Trust [098391/Z/12/Z] Funding Source: researchfish
- BBSRC [BB/J015199/1] Funding Source: UKRI
- Wellcome Trust [101468/Z/13/Z, 090944/Z/09/Z, 105606/Z/14/Z] Funding Source: Wellcome Trust
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During Caenorhabditis elegans oocyte meiosis, a multi-protein ring complex (RC) localized between homologous chromosomes, promotes chromosome congression through the action of the chromokinesin KLP-19. While some RC components are known, the mechanism of RC assembly has remained obscure. We show that SUMO E3 ligase GEI-17/PIAS is required for KLP-19 recruitment to the RC, and proteomic analysis identified KLP-19 as a SUMO substrate in vivo. In vitro analysis revealed that KLP-19 is efficiently sumoylated in a GEI-17-dependent manner, while GEI-17 undergoes extensive auto-sumoylation. GEI-17 and another RC component, the kinase BUB-1, contain functional SUMO interaction motifs (SIMs), allowing them to recruit SUMO modified proteins, including KLP-19, into the RC. Thus, dynamic SUMO modification and the presence of SIMs in RC components generate a SUMO-SIM network that facilitates assembly of the RC. Our results highlight the importance of SUMO-SIM networks in regulating the assembly of dynamic protein complexes.
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