Cátia A. Carvalho

Tel Aviv University

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Limor Broday

Tel Aviv University

Ulrike Bening Abu-Shach

Tel Aviv University

Dan Levy

Ben-Gurion University of the Negev

Asha Raju

Tel Aviv University

Mike Boxem

Utrecht University

Zlata Vershinin

Ben-Gurion University of the Negev

Lirin Michaeli

Tel Aviv University

Cláudio E. Sunkel

Universidade do Porto

Hanna Grobe

Åbo Akademi University

Sofia Moreira

Instituto Gulbenkian de Ciência

Cooperative Institutions

Tel Aviv University

Universidade do Porto

i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto

Instituto de Biologia Molecular e Celular

University of Cambridge

Instituto de Biología Molecular y Celular de Plantas

University of Massachusetts Chan Medical School

Ben-Gurion University of the Negev

National Institutes of Health

Howard Hughes Medical Institute

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Adherens junctions limit the extent of the septate junctions in Drosophila midgut enterocytes but are not required for apical-basal polarity

bioRxiv (Cold Spring Harbor Laboratory) (2024)

Cátia A. Carvalho Mihoko A. Tame Daniel St Johnston

Abstract Adherens junctions formed by E-cadherin adhesion complexes play central roles in the organisation and apical-basal polarisation of both mammalian and insect epithelia. Here we investigate the function of the components of the E-cadherin adhesion complex in the Drosophila midgut epithelium, which establishes polarity by a different mechanism from other fly epithelia and has an inverted junctional arrangement, in which the adherens junctions lie below the septate junctions. Unlike other epithelial tissues, loss of E-cadherin, Armadillo (β-catenin) or α-catenin has no effect on the polarity or organisation of the adult midgut epithelium. This is not due to redundancy with N-cadherin, providing further evidence that the midgut polarises in distinct way from other epithelia. However, E-cadherin ( shg ) and armadillo mutants have an expanded septate junction domain and a smaller lateral domain below the septate junctions. Thus, E-cadherin adhesion complexes limit the basal extent of the septate junctions. This function does not appear to depend on the linkage of E-cadherin to the actin cytoskeleton because α-catenin mutants do not significantly perturb the relative sizes of the septate and sub-septate junction domains.

Adherens junction

Septate junctions

Polarity (international relations)

Basal (medicine)

Septate

10.1101/2024.03.22.586295

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SUMO-mediated regulation of H3K4me3 reader SET-26 controls germline development in C. elegans

PLoS Biology (2025)

Cátia A. Carvalho Ulrike Bening Abu-Shach Asha Raju Zlata Vershinin Dan Levy

Sumoylation is a posttranslational modification essential for multiple cellular functions in eukaryotes. ULP-2 is a conserved SUMO protease required for embryonic development in Caenorhabditis elegans . Here, we revealed that ULP-2 controls germline development by regulating the PHD-SET domain protein, SET-26. Specifically, loss of ULP-2 results in sterility and a progressive elevation of global protein sumoylation. In the germline of ulp-2 null mutant, meiosis is arrested at the diplotene stage and the cells in the proximal germline acquire a somatic fate. Germline RNAseq analysis revealed the down-regulation of numerous germline genes in ulp-2 mutants, whereas somatic gene expression is up-regulated. To determine the key factors that are regulated by ULP-2, we performed a yeast two-hybrid screen and identified the histone methylation reader, SET-26 as a ULP-2 interacting protein. Loss of SET-26 enhanced the sterility of ulp-2 mutant animals. Consistently, SET-26 is sumoylated and its sumoylation levels are regulated by ULP-2. Moreover, we detected a reduction in H3K4 tri-methylation (H3K4me3) histone levels bound to SET-26 in the ulp-2 mutant background suggesting a dependence of this histone reader on balanced sumoylation. Finally, a comparative proteomics screen between WT and ulp-2 loss of activity identified the predicted methyltransferase SET-27 as a ULP-2-dependent SET-26-associated protein. SET-27 knockout genetically interacts with ULP-2 in the germline, but not with SET-26. Taken together, we revealed a SUMO protease/H3K4me3 histone reader axis which is required for the maintenance and regulation of germline development.

H3K4me3

10.1371/journal.pbio.3002980

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ULP-2 SUMO protease regulates UPRmt and mitochondrial homeostasis in Caenorhabditis elegans

Free Radical Biology and Medicine (2024)

Lirin Michaeli Eyal Spector Simon Haeussler Cátia A. Carvalho Hanna Grobe

DNAJA3

Mitochondrial ROS

10.1016/j.freeradbiomed.2024.01.050

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Aurora A Triggers Lgl Cortical Release during Symmetric Division to Control Planar Spindle Orientation

Current Biology (2014)

Cátia A. Carvalho Sofia Moreira Guilherme Ventura Cláudio E. Sunkel Eurico Morais‐de‐Sá

Cell polarity

Asymmetric cell division

Cell Cortex

Cell fate determination

Spindle pole body

10.1016/j.cub.2014.10.053

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Citations (80)

Game of Tissues: How the Epidermis Thrones C. elegans Shape

Journal of Developmental Biology (2020)

Cátia A. Carvalho Limor Broday

The versatility of epithelial cell structure is universally exploited by organisms in multiple contexts. Epithelial cells can establish diverse polarized axes within their tridimensional structure which enables them to flexibly communicate with their neighbors in a 360° range. Hence, these cells are central to multicellularity, and participate in diverse biological processes such as organismal development, growth or immune response and their misfunction ultimately impacts disease. During the development of an organism, the first task epidermal cells must complete is the formation of a continuous sheet, which initiates its own morphogenic process. In this review, we will focus on the C. elegans embryonic epithelial morphogenesis. We will describe how its formation, maturation, and spatial arrangements set the final shape of the nematode C. elegans. Special importance will be given to the tissue-tissue interactions, regulatory tissue-tissue feedback mechanisms and the players orchestrating the process.

Multicellular organism

Epidermis (zoology)

Embryonic Induction

10.3390/jdb8010007

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Citations (15)

SUMO-mediated regulation of a H3K4me3 reader controls germline development inC. elegans

bioRxiv (Cold Spring Harbor Laboratory) (2024)

Cátia A. Carvalho Ulrike Bening Abu-Shach Asha Raju Zlata Vershinin Dan Levy

Abstract ULP-2 is a conserved SUMO protease required for embryonic development in C. elegans . Here we revealed that ULP-2 controls germline development by regulating the PHD-SET domain protein, SET-26. Specifically, the ulp-2 mutant hermaphrodites exhibit increased sterility and progressive elevation in global protein sumoylation. In the progeny of homozygous animals, meiosis is arrested at the diplotene stage and the cells in the proximal germline acquire a somatic fate. Germline RNAseq analysis revealed the downregulation of numerous germline genes, whereas somatic gene expression is upregulated in ulp-2 mutant gonads. To determine the key factors that are regulated by ULP-2, we performed a yeast two-hybrid screen and identified the H3K4me3 reader, SET-26. Genetic interaction was observed in double mutant ulp-2 ; set-26 resulting in enhanced sterility phenotype to complete sterility in the first generation of homozygous offspring. Consistently, SET-26 is sumoylated and its sumoylation levels are regulated by ULP-2. Moreover, we detected reduction in H3K4me3 levels bound to SET-26 in the ulp-2 mutant background. A comparative proteomics screen between WT and ulp-2 loss of activity identified the predicted methyltransferase SET-27 as a ULP-2-dependent SET-26-associated protein. SET-27 knockout genetically interacts with ULP-2 in the germline, but not with SET-26. Taken together, we revealed a ULP-2/SET-26 axis which is required for the maintenance and regulation of germline development.

H3K4me3

10.1101/2024.02.27.582283

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