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Article ; Online: Chromosome segregation during female meiosis in C. elegans: A tale of pushing and pulling.

Taylor, Samuel J P / Pelisch, Federico

2020 Volume 219, Issue 12

Abstract: The role of the kinetochore during meiotic chromosome segregation in C. elegans oocytes has been a matter of controversy. Danlasky et al. (2020. J. Cell. Biol.https://doi.org/10.1083/jcb.202005179) show that kinetochore proteins KNL-1 and KNL-3 are ... ...

Abstract	The role of the kinetochore during meiotic chromosome segregation in C. elegans oocytes has been a matter of controversy. Danlasky et al. (2020. J. Cell. Biol.https://doi.org/10.1083/jcb.202005179) show that kinetochore proteins KNL-1 and KNL-3 are required for early stages of anaphase during female meiosis, suggesting a new kinetochore-based model of chromosome segregation.
MeSH term(s)	Anaphase ; Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans Proteins/genetics ; Chromosome Segregation ; Female ; Kinetochores ; Meiosis ; Microtubule-Associated Proteins/genetics ; Oocytes
Chemical Substances	Caenorhabditis elegans Proteins ; KNL-1 protein, C elegans ; Microtubule-Associated Proteins
Language	English
Publishing date	2020-11-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202011035
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Article ; Online: SUMO promotes longevity and maintains mitochondrial homeostasis during ageing in Caenorhabditis elegans.

Princz, Andrea / Pelisch, Federico / Tavernarakis, Nektarios

Scientific reports

2020 Volume 10, Issue 1, Page(s) 15513

Abstract: The insulin/IGF signalling pathway impacts lifespan across distant taxa, by controlling the activity of nodal transcription factors. In the nematode Caenorhabditis elegans, the transcription regulators DAF-16/FOXO and SKN-1/Nrf function to promote ... ...

Abstract	The insulin/IGF signalling pathway impacts lifespan across distant taxa, by controlling the activity of nodal transcription factors. In the nematode Caenorhabditis elegans, the transcription regulators DAF-16/FOXO and SKN-1/Nrf function to promote longevity under conditions of low insulin/IGF signalling and stress. The activity and subcellular localization of both DAF-16 and SKN-1 is further modulated by specific posttranslational modifications, such as phosphorylation and ubiquitination. Here, we show that ageing elicits a marked increase of SUMO levels in C. elegans. In turn, SUMO fine-tunes DAF-16 and SKN-1 activity in specific C. elegans somatic tissues, to enhance stress resistance. SUMOylation of DAF-16 modulates mitochondrial homeostasis by interfering with mitochondrial dynamics and mitophagy. Our findings reveal that SUMO is an important determinant of lifespan, and provide novel insight, relevant to the complexity of the signalling mechanisms that influence gene expression to govern organismal survival in metazoans.
MeSH term(s)	Aging/metabolism ; Aging/physiology ; Animals ; Blotting, Western ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/metabolism ; Caenorhabditis elegans Proteins/physiology ; Cloning, Molecular ; DNA, Mitochondrial/metabolism ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/physiology ; Forkhead Transcription Factors/metabolism ; Forkhead Transcription Factors/physiology ; Gene Expression Regulation, Developmental ; Homeostasis/physiology ; Longevity/physiology ; Mitochondria/metabolism ; Mitochondria/physiology ; Oxygen Consumption ; SUMO-1 Protein/metabolism ; SUMO-1 Protein/physiology ; Sumoylation ; Transcription Factors/metabolism ; Transcription Factors/physiology
Chemical Substances	Caenorhabditis elegans Proteins ; DNA, Mitochondrial ; DNA-Binding Proteins ; Forkhead Transcription Factors ; SUMO-1 Protein ; Transcription Factors ; daf-16 protein, C elegans ; skn-1 protein, C elegans (148733-36-2)
Language	English
Publishing date	2020-09-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-72637-9
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Article ; Online: BUB-1 and CENP-C recruit PLK-1 to control chromosome alignment and segregation during meiosis I in

Taylor, Samuel J P / Bel Borja, Laura / Soubigou, Flavie / Houston, Jack / Cheerambathur, Dhanya K / Pelisch, Federico

eLife

2023 Volume 12

Abstract: Phosphorylation is a key post-translational modification that is utilised in many biological processes for the rapid and reversible regulation of protein localisation and activity. Polo-like kinase 1 (PLK-1) is essential for both mitotic and meiotic cell ...

Abstract	Phosphorylation is a key post-translational modification that is utilised in many biological processes for the rapid and reversible regulation of protein localisation and activity. Polo-like kinase 1 (PLK-1) is essential for both mitotic and meiotic cell divisions, with key functions being conserved in eukaryotes. The roles and regulation of PLK-1 during mitosis have been well characterised. However, the discrete roles and regulation of PLK-1 during meiosis have remained obscure. Here, we used
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Chromosome Segregation ; Kinetochores ; Meiosis ; Oocytes ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Spindle Apparatus/metabolism ; Polo-Like Kinase 1
Chemical Substances	Caenorhabditis elegans Proteins ; centromere protein C ; plk-1 protein, C elegans (EC 2.7.11.21) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; bub-1 protein, C elegans (EC 2.7.11.1)
Language	English
Publishing date	2023-04-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.84057
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Article ; Online: Tools to Study SUMO Conjugation in Caenorhabditis elegans.

Pelisch, Federico / Hay, Ronald T

Methods in molecular biology (Clifton, N.J.)

2016 Volume 1475, Page(s) 233–256

Abstract: The cell biology of sumoylation has mostly been studied using transformed cultured cells and yeast. In recent years, genetic analysis has demonstrated important roles for sumoylation in the biology of C. elegans. Here, we expand the existing set of tools ...

Abstract	The cell biology of sumoylation has mostly been studied using transformed cultured cells and yeast. In recent years, genetic analysis has demonstrated important roles for sumoylation in the biology of C. elegans. Here, we expand the existing set of tools making it possible to address the role of sumoylation in the nematode C. elegans using a combination of genetics, imaging, and biochemistry. Most importantly, the dynamics of SUMO conjugation and deconjugation can be followed very precisely both in space and time within living worms. Additionally, the biochemistry of SUMO conjugation and deconjugation can be addressed using recombinant purified components of the C. elegans sumoylation machinery, including E3 ligases and SUMO proteases. These tools and reagents will be useful to gain insights into the biological role of SUMO in the context of a multicellular organism.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/biosynthesis ; Antibodies, Monoclonal/chemistry ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans/ultrastructure ; Caenorhabditis elegans Proteins/antagonists & inhibitors ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Division ; Chromosomes/metabolism ; Chromosomes/ultrastructure ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Genes, Reporter ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Humans ; Isoenzymes/antagonists & inhibitors ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Ligases/antagonists & inhibitors ; Ligases/genetics ; Ligases/metabolism ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Plasmids/chemistry ; Plasmids/metabolism ; Protein Processing, Post-Translational ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Small Ubiquitin-Related Modifier Proteins/genetics ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Sumoylation ; Time-Lapse Imaging/methods ; Ubiquitin-Conjugating Enzymes/antagonists & inhibitors ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Conjugating Enzymes/metabolism ; Red Fluorescent Protein
Chemical Substances	Antibodies, Monoclonal ; Caenorhabditis elegans Proteins ; Isoenzymes ; Luminescent Proteins ; RNA, Small Interfering ; Recombinant Fusion Proteins ; Small Ubiquitin-Related Modifier Proteins ; Green Fluorescent Proteins (147336-22-9) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Cysteine Endopeptidases (EC 3.4.22.-) ; Ulp1 protease (EC 3.4.22.-) ; GEI-17 protein, C elegans (EC 6.-) ; Ligases (EC 6.-)
Language	English
Publishing date	2016-11-14
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-6358-4_17
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Article ; Online: Author Correction: Dynamic SUMO modification regulates mitotic chromosome assembly and cell cycle progression in Caenorhabditis elegans.

Pelisch, Federico / Sonneville, Remi / Pourkarimi, Ehsan / Agostinho, Ana / Blow, J Julian / Gartner, Anton / Hay, Ronald T

Nature communications

2022 Volume 13, Issue 1, Page(s) 7220

Language	English
Publishing date	2022-11-24
Publishing country	England
Document type	Published Erratum
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-35079-7
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Article ; Online: Sumoylation regulates protein dynamics during meiotic chromosome segregation in

Pelisch, Federico / Bel Borja, Laura / Jaffray, Ellis G / Hay, Ronald T

Journal of cell science

2019 Volume 132, Issue 14

Abstract: Oocyte meiotic spindles in most species lack centrosomes and the mechanisms that underlie faithful chromosome segregation in acentrosomal meiotic spindles are not well understood. ... ...

Abstract	Oocyte meiotic spindles in most species lack centrosomes and the mechanisms that underlie faithful chromosome segregation in acentrosomal meiotic spindles are not well understood. In
MeSH term(s)	Anaphase ; Animals ; Caenorhabditis elegans/cytology ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Chromosome Segregation ; Meiosis ; Models, Biological ; Oocytes/cytology ; Oocytes/metabolism ; Protein Transport ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Spindle Apparatus/metabolism ; Sumoylation
Chemical Substances	Caenorhabditis elegans Proteins ; Small Ubiquitin-Related Modifier Proteins
Language	English
Publishing date	2019-07-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.232330
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Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Tools to Study SUMO Conjugation in Caenorhabditis elegans

Pelisch, Federico / Hay, Ronald T.

Jahrbuch der Psychoanalyse

2016 Volume 73, Issue -, Page(s) 233

Language	German
Document type	Article
ZDB-ID	184280-8
ISSN	0075-2363
Database	Current Contents Medicine

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Article ; Conference proceedings: A SUMO-Dependent Protein Network Regulates Chromosome Congression during Oocyte Meiosis

Pelisch, Federico / Anton Gartner / Bin Wang / Ellis G. Jaffray / Ronald T. Hay / Triin Tammsalu

Molecular cell. 2017 Jan. 05, v. 65, no. 1

2017

Abstract: 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 ...

Abstract	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.
Keywords	Caenorhabditis elegans ; chromosomes ; meiosis ; oocytes ; proteins ; proteomics ; ubiquitin-protein ligase
Language	English
Dates of publication	2017-0105
Size	p. 66-77.
Publishing place	Elsevier Inc.
Document type	Article ; Conference proceedings
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2016.11.001
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: RNA metabolism and ubiquitin/ubiquitin-like modifications collide.

Pelisch, Federico / Risso, Guillermo / Srebrow, Anabella

Briefings in functional genomics

2013 Volume 12, Issue 1, Page(s) 66–71

Abstract: Alternative splicing and post-translational modifications are key events for the generation of proteome diversity in eukaryotes. The study of the molecular mechanisms governing these processes, and every other step of gene expression, has underscored the ...

Abstract	Alternative splicing and post-translational modifications are key events for the generation of proteome diversity in eukaryotes. The study of the molecular mechanisms governing these processes, and every other step of gene expression, has underscored the existing interconnectedness among them. Therefore, molecules that could concertedly regulate different stages from transcription to pre-mRNA processing, translation and even protein activity have called our attention. Serine/arginine-rich proteins, initially identified as splicing regulators, are involved in diverse aspects of gene expression. Although most of the roles exerted by members of this family are related to mRNA biogenesis and metabolism, few recently uncovered ones link these proteins to other regulatory steps along gene expression, particularly the regulation of post-translational modification by conjugation of the small ubiquitin-related modifier. This along with the established link between ubiquitin, transcription and pre-mRNA processing points to a general mechanism of interaction between different cellular machineries, such as ubiquitin/ubiquitin-like conjugation pathways, transcription apparatus and the spliceosome.
MeSH term(s)	Alternative Splicing/genetics ; Animals ; Humans ; Models, Biological ; Protein Processing, Post-Translational/genetics ; RNA/genetics ; RNA/metabolism ; Ubiquitin/metabolism
Chemical Substances	Ubiquitin ; RNA (63231-63-0)
Language	English
Publishing date	2013-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2540916-5
ISSN	2041-2657 ; 2041-2649 ; 2041-2647
ISSN (online)	2041-2657
ISSN	2041-2649 ; 2041-2647
DOI	10.1093/bfgp/els053
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Article ; Online: A SUMO-Dependent Protein Network Regulates Chromosome Congression during Oocyte Meiosis.

Pelisch, Federico / Tammsalu, Triin / Wang, Bin / Jaffray, Ellis G / Gartner, Anton / Hay, Ronald T

Molecular cell

2016 Volume 65, Issue 1, Page(s) 66–77

Abstract	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.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Chromosome Positioning ; Chromosome Segregation ; Female ; Genotype ; Kinesins/genetics ; Kinesins/metabolism ; Ligases/genetics ; Ligases/metabolism ; Meiosis ; Oocytes/metabolism ; Phenotype ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Signal Transduction ; Sumoylation ; Time Factors ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; KLP-19 protein, C elegans ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; bub-1 protein, C elegans (EC 2.7.11.1) ; Kinesins (EC 3.6.4.4) ; GEI-17 protein, C elegans (EC 6.-) ; Ligases (EC 6.-)
Language	English
Publishing date	2016-12-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2016.11.001
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