Germ Cell Fate Determination in
            <scp>
              <i>C. e</i>
            </scp>
            <i>legans</i>

Voronina, Ekaterina; Greenstein, David

doi:10.1002/9780470015902.a0001501.pub2

Cited by 3 publications

(1 citation statement)

References 54 publications

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“…SPCs are maintained through the GLP-1/Notch signaling from the somatic niche cell (Austin and Kimble, 1987; Berry et al, 1997; Kimble and Crittenden, 2007). As the cells progress away from the niche, they begin to differentiate and enter meiosis before generating gametes at the proximal end (Hubbard, 2007; Pazdernik and Schedl, 2013; Voronina and Greenstein, 2016). The germlines produce sperm during larval development and switch to oogenesis in the young adults (Pazdernik and Schedl, 2013).…”

Section: Introductionmentioning

confidence: 99%

COP9 signalosome component CSN-5 stabilizes PUF proteins FBF-1 and FBF-2 inCaenorhabditis elegansgermline stem cells

Osterli

Ellenbecker

Wang

et al. 2022

Preprint

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RNA-binding proteins FBF-1 and FBF-2 (FBFs) are required for germline stem cell maintenance in Caenorhabditis elegans and regulate the dynamics of progenitor cell proliferation and differentiation. The mechanisms controlling FBF protein levels remain unknown. We identified an interaction between both FBFs and CSN-5, a component of the COP9 (constitutive photomorphogenesis 9) signalosome. Here, we find that the MPN (Mpr1/Pad1 N-terminal) metalloprotease domain of CSN-5 interacts with the PUF RNA-binding domain of FBFs and the interaction is conserved for human homologs hPUM1 and hCSN5. This interaction likely takes place outside of the COP9 holoenzyme. csn-5 mutation results in destabilization of FBF proteins in germline stem cells leading to phenotypes consistent with a partial FBF loss of function. We propose that a COP9-independent role of CSN-5 in the PUF protein stability and function may be conserved across species, with implications for human stem cell biology and cancer.

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Section: Introductionmentioning

confidence: 99%

COP9 signalosome component CSN-5 stabilizes PUF proteins FBF-1 and FBF-2 inCaenorhabditis elegansgermline stem cells

Osterli

Ellenbecker

Wang

et al. 2022

Preprint

Self Cite

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COP9 signalosome component CSN-5 stabilizes PUF proteins FBF-1 and FBF-2 in Caenorhabditis elegans germline stem and progenitor cells

Osterli,

Ellenbecker,

Wang

et al. 2024

Genetics

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RNA-binding proteins FBF-1 and FBF-2 (FBFs) are required for germline stem cell maintenance and the sperm/oocyte switch in Caenorhabditis elegans, though the mechanisms controlling FBF protein levels remain unknown. We identified an interaction between both FBFs and CSN-5, a component of the COP9 (constitutive photomorphogenesis 9) signalosome best known for its role in regulating protein degradation. Here, we find that the Mpr1/Pad1 N-terminal metalloprotease domain of CSN-5 interacts with the Pumilio and FBF RNA-binding domain of FBFs and the interaction is conserved for human homologs CSN5 and PUM1. The interaction between FBF-2 and CSN-5 can be detected in vivo by proximity ligation. csn-5 mutation results in destabilization of FBF proteins, that may explain previously observed decrease in the numbers of germline stem and progenitor cells, and disruption of oogenesis. The loss of csn-5 does not decrease the levels of a related PUF protein PUF-3 and csn-5(lf) phenotype is not enhanced by fbf-1/2 knockdown, suggesting that the effect is specific to FBFs. The effect of csn-5 on oogenesis is largely independent of the COP9 signalosome and is cell autonomous. Surprisingly, regulation of FBF protein levels involves a combination of COP9-dependent and –independent mechanisms differentially affecting FBF-1 and FBF-2. This work supports a previously unappreciated role for CSN-5 in stabilization of germline stem cell regulatory proteins FBF-1 and FBF-2.

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Dynein Light Chain DLC-1 Facilitates the Function of the Germline Cell Fate Regulator GLD-1 in Caenorhabditis elegans

Ellenbecker¹,

Osterli²,

Wang³

et al. 2018

Genetics

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Developmental transitions of germ cells are often regulated at the level of post-transcriptional control of gene expression. In the Caenorhabditis elegans germline, stem and progenitor cells exit the proliferative phase and enter meiotic differentiation to form gametes essential for fertility. The RNA binding protein GLD-1 is a cell fate regulator that promotes meiosis and germ cell differentiation during development by binding to and repressing translation of target messenger RNAs. Here, we discovered that some GLD-1 functions are promoted by binding to DLC-1, a small protein that functions as an allosteric regulator of multisubunit protein complexes. We found that DLC-1 is required to regulate a subset of GLD-1 target messenger RNAs and that DLC-1 binding GLD-1 prevents ectopic germ cell proliferation and facilitates gametogenesis in vivo. Additionally, our results reveal a new requirement for GLD-1 in the events of oogenesis leading to ovulation. DLC-1 contributes to GLD-1 function independent of its role as a light chain component of the dynein motor. Instead, we propose that DLC-1 promotes assembly of GLD-1 with other binding partners, which facilitates formation of regulatory ribonucleoprotein complexes and may direct GLD-1 target messenger RNA selectivity.

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Germ Cell Fate Determination in C. e legans

Cited by 3 publications

References 54 publications

COP9 signalosome component CSN-5 stabilizes PUF proteins FBF-1 and FBF-2 inCaenorhabditis elegansgermline stem cells

COP9 signalosome component CSN-5 stabilizes PUF proteins FBF-1 and FBF-2 inCaenorhabditis elegansgermline stem cells

COP9 signalosome component CSN-5 stabilizes PUF proteins FBF-1 and FBF-2 in Caenorhabditis elegans germline stem and progenitor cells

Dynein Light Chain DLC-1 Facilitates the Function of the Germline Cell Fate Regulator GLD-1 in Caenorhabditis elegans

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