Faculty Opinions recommendation of P granules extend the nuclear pore complex environment in the C. elegans germ line.

2015 ◽  
Author(s):  
Florence Marlow
Keyword(s):  
Nuclear Pore Complex ◽  
Germ Line ◽  
Nuclear Pore ◽  
Complex Environment ◽  
P Granules ◽  
C Elegans

scholarly journals P granules extend the nuclear pore complex environment in the C. elegans germ line

2011 ◽  
Vol 192 (6) ◽  
pp. 939-948 ◽  
Author(s):  
Dustin L. Updike ◽  
Stephanie J. Hachey ◽  
Jeremy Kreher ◽  
Susan Strome
Keyword(s):  
Nuclear Pore Complex ◽  
Germ Plasm ◽  
Germ Line ◽  
Hydrophobic Interactions ◽  
Nuclear Periphery ◽  
Size Exclusion ◽  
Nuclear Pore ◽  
Complex Environment ◽  
P Granules ◽  
C Elegans

The immortal and totipotent properties of the germ line depend on determinants within the germ plasm. A common characteristic of germ plasm across phyla is the presence of germ granules, including P granules in Caenorhabditis elegans, which are typically associated with the nuclear periphery. In C. elegans, nuclear pore complex (NPC)–like FG repeat domains are found in the VASA-related P-granule proteins GLH-1, GLH-2, and GLH-4 and other P-granule components. We demonstrate that P granules, like NPCs, are held together by weak hydrophobic interactions and establish a size-exclusion barrier. Our analysis of intestine-expressed proteins revealed that GLH-1 and its FG domain are not sufficient to form granules, but require factors like PGL-1 to nucleate the localized concentration of GLH proteins. GLH-1 is necessary but not sufficient for the perinuclear location of granules in the intestine. Our results suggest that P granules extend the NPC environment in the germ line and provide insights into the roles of the PGL and GLH family proteins.

scholarly journals Novel LOTUS-domain proteins are organizational hubs that recruit C. elegans Vasa to germ granules

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Patricia Giselle Cipriani ◽  
Olivia Bay ◽  
John Zinno ◽  
Michelle Gutwein ◽  
Hin Hark Gan ◽  
...  
Keyword(s):  
Rna Processing ◽  
Germ Line ◽  
Temperature Sensitive ◽  
Developmental Transitions ◽  
P Granules ◽  
C Elegans ◽  
Intrinsically Disordered ◽  
Meiotic Progression ◽  
Intrinsically Disordered Regions ◽  
Granule Growth

We describe MIP-1 and MIP-2, novel paralogous C. elegans germ granule components that interact with the intrinsically disordered MEG-3 protein. These proteins promote P granule condensation, form granules independently of MEG-3 in the postembryonic germ line, and balance each other in regulating P granule growth and localization. MIP-1 and MIP-2 each contain two LOTUS domains and intrinsically disordered regions and form homo- and heterodimers. They bind and anchor the Vasa homolog GLH-1 within P granules and are jointly required for coalescence of MEG-3, GLH-1, and PGL proteins. Animals lacking MIP-1 and MIP-2 show temperature-sensitive embryonic lethality, sterility, and mortal germ lines. Germline phenotypes include defects in stem cell self-renewal, meiotic progression, and gamete differentiation. We propose that these proteins serve as scaffolds and organizing centers for ribonucleoprotein networks within P granules that help recruit and balance essential RNA processing machinery to regulate key developmental transitions in the germ line.

scholarly journals Proximity labeling identifies LOTUS domain proteins that promote the formation of perinuclear germ granules in C. elegans

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Ian F Price ◽  
Hannah L Hertz ◽  
Benjamin Pastore ◽  
Jillian Wagner ◽  
Wen Tang
Keyword(s):  
Germ Line ◽  
Nuclear Periphery ◽  
P Granules ◽  
C Elegans ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Germ Granules ◽  
Protein Components ◽  
Labeling Method ◽  
Disordered Regions

The germ line produces gametes that transmit genetic and epigenetic information to the next generation. Maintenance of germ cells and development of gametes require germ granules-well-conserved membraneless and RNA-rich organelles. The composition of germ granules is elusive owing to their dynamic nature and their exclusive expression in the germ line. Using C. elegans germ granule, called P granule, as a model system, we employed a proximity-based labeling method in combination with mass spectrometry to comprehensively define its protein components. This set of experiments identified over 200 proteins, many of which contain intrinsically disordered regions. An RNAi-based screen identified factors that are essential for P granule assembly, notably EGGD-1 and EGGD-2, two putative LOTUS-domain proteins. Loss of eggd-1 and eggd-2 results in separation of P granules from the nuclear envelope, germline atrophy and reduced fertility. We show that intrinsically disordered regions of EGGD-1 are required to anchor EGGD-1 to the nuclear periphery while its LOTUS domains are required to promote perinuclear localization of P granules. Together, our work expands the repertoire of P granule constituents and provides new insights into the role of LOTUS-domain proteins in germ granule organization.

Germline and developmental roles of the nuclear transport factor importin (α)3 in C. elegans

Development ◽  
2001 ◽  
Vol 128 (10) ◽  
pp. 1817-1830 ◽  
Author(s):  
K.G. Geles ◽  
S.A. Adam
Keyword(s):  
Nuclear Transport ◽  
Intracellular Localization ◽  
Nuclear Pore ◽  
P Granules ◽  
C Elegans ◽  
Cellular Events ◽  
Importin Α ◽  
Localization Signal ◽  
Transport Factors ◽  
Embryonic And Larval Development

The importin (α) family of transport factors mediates the nuclear import of classical nuclear localization signal-containing proteins. In order to understand how multiple importin (α) proteins are regulated both in individual cells and in a whole organism, the three importin (α) (ima) genes of Caenorhabditis elegans have been identified and studied. All three IMAs are expressed in the germline; however, only IMA-3 is expressed in the soma. RNA interference (RNAi) experiments demonstrate that IMA-3 is required for the progression of meiotic prophase I during oocyte development. Loss of IMA-3 expression leads also to a disruption of the nuclear pore complex accompanied by the mis-localization of P granules. A range of defects occurring in ima-3(RNAi) F(1) progeny further supports a role for IMA-3 during embryonic and larval development. The functional association of IMA-3 with distinct cellular events, its expression pattern and intracellular localization indicate that regulation of the nuclear transport machinery is involved in the control of developmental pathways.

PAR-2 is asymmetrically distributed and promotes association of P granules and PAR-1 with the cortex in C. elegans embryos

Development ◽  
1996 ◽  
Vol 122 (10) ◽  
pp. 3075-3084 ◽  
Author(s):  
L. Boyd ◽  
S. Guo ◽  
D. Levitan ◽  
D.T. Stinchcomb ◽  
K.J. Kemphues
Keyword(s):  
Cell Cycle ◽  
Germ Line ◽  
Cell Cortex ◽  
Asymmetric Distribution ◽  
Cell Stage ◽  
Posterior Cortex ◽  
P Granules ◽  
C Elegans ◽  
Cortical Localization ◽  
The One

The par genes participate in the process of establishing cellular asymmetries during the first cell cycle of Caenorhabditis elegans development. The par-2 gene is required for the unequal first cleavage and for asymmetries in cell cycle length and spindle orientation in the two resulting daughter cells. We have found that the PAR-2 protein is present in adult gonads and early embryos. In gonads, the protein is uniformly distributed at the cell cortex, and this subcellular localization depends on microfilaments. In the one-cell embryo, PAR-2 is localized to the posterior cortex and is partitioned into the posterior daughter, P1, at the first cleavage. PAR-2 exhibits a similar asymmetric cortical localization in P1, P2, and P3, the asymmetrically dividing blastomeres of germ line lineage. This distribution in embryos is very similar to that of PAR-1 protein. By analyzing the distribution of the PAR-2 protein in various par mutant backgrounds we found that proper asymmetric distribution of PAR-2 depends upon par-3 activity but not upon par-1 or par-4. par-2 activity is required for proper cortical localization of PAR-1 and this effect requires wild-type par-3 gene activity. We also find that, although par-2 activity is not required for posterior localization of P granules at the one-cell stage, it is required for proper cortical association of P granules in P1.

scholarly journals Characterization and Targeted Disruption of Murine Nup50, a p27Kip1-Interacting Component of the Nuclear Pore Complex

2000 ◽  
Vol 20 (15) ◽  
pp. 5631-5642 ◽  
Author(s):  
Matthew Smitherman ◽  
Keesook Lee ◽  
Jherek Swanger ◽  
Raj Kapur ◽  
Bruce E. Clurman
Keyword(s):  
Neural Tube ◽  
Nuclear Pore Complex ◽  
Mammalian Cells ◽  
Germ Line ◽  
Nuclear Pore ◽  
Null Mouse ◽  
Mouse Development ◽  
Genomic Locus ◽  
Two Hybrid

ABSTRACT p27Kip1 is a member of the Cip-Kip family of cyclin-dependent kinase (Cdk) inhibitors that binds to cyclin-Cdk complexes and inhibits their catalytic activity in response to antiproliferative stimuli. p27Kip1 is regulated by several posttranscriptional mechanisms, including subcellular localization. We have identified a component of the nuclear pore complex (NPC), termed Nup50, through its two-hybrid interactions with p27Kip1. Nup50 is a nucleoplasmically oriented component of the nuclear pore complex with a role in protein export (T. Guan, R. H. Kehlenbach, E. C. Schirmer, A. Kehlenbach, F. Fan, B. E. Clurman, N. Arnheim, and L. Gerace, Mol. Cell. Biol. 20:5619–5630, 2000). We found that murine Nup50 is a widely expressed nucleoporin and that Nup50 expression is highest in the developing neural tube and adult testes. We have also examined interactions between Nup50 and the NPC and found specific two-hybrid interactions between Nup50 and several well-defined components of the NPC, as well as coimmunoprecipitation of Nup50 with the nucleoporin Nup153 from transfected mammalian cells. In order to study Nup50 function in vivo, we cloned the mouse Nup50 genomic locus and created a targeted Nup50 deletion in the mouse germ line. Nup50 disruption resulted in a complex phenotype characterized by late embryonic lethality, neural tube defects, and intrauterine growth retardation. Although Nup50-null mouse embryo fibroblasts exhibited no defects in either cell cycle control or p27Kip1 regulation, Nup50 deletion was associated with abnormalities in p27Kip1expression and cell proliferation in the developing neuroepithelium. We conclude that Nup50 is a nucleoporin with essential functions during mouse development.

scholarly journals Novel LOTUS-domain proteins are organizational hubs that recruit C. elegans Vasa to germ granules

2021 ◽  
Author(s):  
Patricia Giselle Cipriani ◽  
Olivia Bay ◽  
John Peter Zinno ◽  
Michelle Gutwein ◽  
Hin Hark Gan ◽  
...  
Keyword(s):  
Rna Processing ◽  
Germ Line ◽  
Temperature Sensitive ◽  
Developmental Transitions ◽  
P Granules ◽  
C Elegans ◽  
Intrinsically Disordered ◽  
Meiotic Progression ◽  
Intrinsically Disordered Regions ◽  
Granule Growth

We describe MIP-1 and MIP-2, novel paralogous C. elegans germ granule components that interact with the intrinsically disordered MEG-3 protein. These proteins promote P granule condensation, form granules independently of MEG-3 in the postembryonic germ line and balance each other in regulating P granule growth and localization. MIP-1 and MIP-2 each contain two LOTUS domains and intrinsically disordered regions and form homo- and heterodimers. They bind and anchor the Vasa homolog GLH-1 within P granules and are jointly required for coalescence of MEG-3, GLH-1, and PGL proteins. Animals lacking MIP-1 and MIP-2 show temperature-sensitive embryonic lethality, sterility, and mortal germ lines. Germline phenotypes include defects in stem cell self-renewal, meiotic progression, and gamete differentiation. We propose that these proteins serve as scaffolds and organizing centers for ribonucleoprotein networks within P granules that help recruit and balance essential RNA processing machinery to regulate key developmental transitions in the germ line.

scholarly journals Sm protein down-regulation leads to defects in nuclear pore complex disassembly and distribution in C. elegans embryos

2012 ◽  
Vol 365 (2) ◽  
pp. 445-457 ◽  
Author(s):  
Daphna Joseph-Strauss ◽  
Mátyás Gorjánácz ◽  
Rachel Santarella-Mellwig ◽  
Ekaterina Voronina ◽  
Anjon Audhya ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Down Regulation ◽  
C Elegans ◽  
Sm Protein

scholarly journals Reevaluation of whether a soma–to–germ-line transformation extends lifespan in Caenorhabditis elegans

2016 ◽  
Vol 113 (13) ◽  
pp. 3591-3596 ◽  
Author(s):  
Andrew Kekūpa'a Knutson ◽  
Andreas Rechtsteiner ◽  
Susan Strome
Keyword(s):  
Young Adults ◽  
Caenorhabditis Elegans ◽  
Germ Line ◽  
Somatic Cells ◽  
Simultaneous Removal ◽  
Whole Genome ◽  
P Granules ◽  
C Elegans ◽  
Granule Proteins ◽  
Germ Line Transformation

The germ lineage is considered to be immortal. In the quest to extend lifespan, a possible strategy is to drive germ-line traits in somatic cells, to try to confer some of the germ lineage’s immortality on the somatic body. Notably, a study in Caenorhabditis elegans suggested that expression of germ-line genes in the somatic cells of long-lived daf-2 mutants confers some of daf-2’s long lifespan. Specifically, mRNAs encoding components of C. elegans germ granules (P granules) were up-regulated in daf-2 mutant worms, and knockdown of individual P-granule and other germ-line genes in daf-2 young adults modestly reduced their lifespan. We investigated the contribution of a germ-line program to daf-2’s long lifespan and also tested whether other mutants known to express germ-line genes in their somatic cells are long-lived. Our key findings are as follows. (i) We could not detect P-granule proteins in the somatic cells of daf-2 mutants by immunostaining or by expression of a P-granule transgene. (ii) Whole-genome transcript profiling of animals lacking a germ line revealed that germ-line transcripts are not up-regulated in the soma of daf-2 worms compared with the soma of control worms. (iii) Simultaneous removal of multiple P-granule proteins or the entire germ-line program from daf-2 worms did not reduce their lifespan. (iv) Several mutants that robustly express a broad spectrum of germ-line genes in their somatic cells are not long-lived. Together, our findings argue against the hypothesis that acquisition of a germ-cell program in somatic cells increases lifespan and contributes to daf-2’s long lifespan.

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