The E3 Ubiquitin Ligase MIB-1 Is Necessary To Form the Nuclear Halo in <i>Caenorhabditis elegans</i> Sperm

Herrera, Leslie A; Starr, Daniel A.

doi:10.1534/g3.118.200426

Cited by 4 publications

(2 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We collected genomic DNA from each homozygous mutant strain for whole-genome sequencing to identify candidate lesions underlying the nuclear migration phenotypes. Genomic DNA preps were made with the Qiagen DNeasy Blood and Tissue kit as previously described ( Herrera and Starr, 2018 ). Genomic DNA was fragmented and made into libraries for Illumina HiSeq2500 sequencing by the Functional Genomics Laboratory at UC Berkeley.…”

Section: Methodsmentioning

confidence: 99%

Actin and CDC-42 contribute to nuclear migration through constricted spaces in C. elegans

Ho,

Guerrero,

Libuda

et al. 2023

Development

View full text Add to dashboard Cite

Successful nuclear migration through constricted spaces between cells or in the extracellular matrix relies on the ability of the nucleus to deform. Little is known about how this takes place in vivo. We have studied confined nuclear migration in Caenorhabditis elegans larval P cells, which is mediated by the LINC complex to pull nuclei towards the minus ends of microtubules. Null mutations of the LINC component unc-84 lead to a temperature-dependent phenotype, suggesting a parallel pathway for P-cell nuclear migration. A forward genetic screen for enhancers of unc-84 identified cgef-1 (CDC-42 guanine nucleotide exchange factor). Knockdown of CDC-42 in the absence of the LINC complex led to a P-cell nuclear migration defect. Expression of constitutively active CDC-42 partially rescued nuclear migration in cgef-1; unc-84 double mutants, suggesting that CDC-42 functions downstream of CGEF-1. The Arp2/3 complex and non-muscle myosin II (NMY-2) were also found to function parallel to the LINC pathway. In our model, CGEF-1 activates CDC-42, which induces actin polymerization through the Arp2/3 complex to deform the nucleus during nuclear migration, and NMY-2 helps to push the nucleus through confined spaces.

show abstract

Section: Methodsmentioning

confidence: 99%

Actin and CDC-42 contribute to nuclear migration through constricted spaces in C. elegans

Ho,

Guerrero,

Libuda

et al. 2023

Development

View full text Add to dashboard Cite

show abstract

“…Like SPE-6, SPE-11 distributes to cytoplasmic granules in mutant sperm that lack chromosomes ( Sadler and Shakes 2000 ). Proper assembly of the perinuclear halo requires the E3 ubiquitin ligase mindbomb ( Herrera and Starr 2018 ; Ratliff et al 2018 ) and the 26G-RNA-related Argonaut proteins ALG-3/4 ( Conine et al 2013 ). Thus our discovery that SPE-6 localizes to the perinuclear halo was surprising since this location places SPE-6 amongst components needed for postfertilization functions and physically apart from known components of the sperm activation pathways.…”

Section: Discussionmentioning

confidence: 99%

Subcellular patterns of SPE-6 localization reveal unexpected complexities inCaenorhabditis eleganssperm activation and sperm function

Peterson

Tocheny

Prajapati

et al. 2021

G3 Genes|Genomes|Genetics

View full text Add to dashboard Cite

To acquire and maintain directed cell motility, Caenorhabditis elegans sperm must undergo extensive, regulated cellular remodeling, in the absence of new transcription or translation. To regulate sperm function, nematode sperm employ large numbers of protein kinases and phosphatases, including SPE-6, a member of C. elegans’ highly expanded casein kinase 1 superfamily. SPE-6 functions during multiple steps of spermatogenesis, including functioning as a “brake” to prevent premature sperm activation in the absence of normal extracellular signals. Here we describe the sub-cellular localization patterns of SPE-6 during wildtype C. elegans sperm development and in various sperm activation mutants. While other members of the sperm activation pathway associate with the plasma membrane or localize to the sperm’s membranous organelles, SPE-6 surrounds the chromatin mass of unactivated sperm. During sperm activation by either of two semiautonomous signaling pathways, SPE-6 redistributes to the front, central region of the sperm’s pseudopod. When disrupted by reduction-of-function alleles, SPE-6 protein is either diminished in a temperature-sensitive manner (hc187) or is mis-localized in a stage-specific manner (hc163). During the multistep process of sperm activation, SPE-6 is released from its perinuclear location after the spike stage in a process that does not require fusion of membranous organelles with the plasma membrane. After activation, spermatozoa exhibit variable proportions of perinuclear and pseudopod-localized SPE-6, depending on their location within the female reproductive tract. These findings provide new insights regarding SPE-6’s role in sperm activation and suggest that extracellular signals during sperm migration may further modulate SPE-6 localization and function.

show abstract

E3 ubiquitin ligase Mindbomb 1 facilitates nuclear delivery of adenovirus genomes

Sarbanes

Blomen

Lam

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The journey from plasma membrane to nuclear pore is a critical step in the lifecycle of DNA viruses, many of which must successfully deposit their genomes into the nucleus for replication. Viral capsids navigate this vast distance through the coordinated hijacking of a number of cellular host factors, many of which remain unknown. We performed a gene-trap screen in haploid cells to identify host factors for adenovirus (AdV), a DNA virus that can cause severe respiratory illness in immune-compromised individuals. This work identified Mindbomb 1 (MIB1), an E3 ubiquitin ligase involved in neurodevelopment, as critical for AdV infectivity. In the absence of MIB1, we observed that viral capsids successfully traffic to the proximity of the nucleus but ultimately fail to deposit their genomes within. The capacity of MIB1 to promote AdV infection was dependent on its ubiquitination activity, suggesting that MIB1 may mediate proteasomal degradation of one or more negative regulators of AdV infection. Employing complementary proteomic approaches to characterize proteins proximal to MIB1 upon AdV infection and differentially ubiquitinated in the presence or absence of MIB1, we observed an intersection between MIB1 and ribonucleoproteins (RNPs) largely unexplored in mammalian cells. This work uncovers yet another way that viruses utilize host cell machinery for their own replication, highlighting a potential target for therapeutic interventions that counter AdV infection.

show abstract

The E3 Ubiquitin Ligase MIB-1 Is Necessary To Form the Nuclear Halo in Caenorhabditis elegans Sperm

Cited by 4 publications

References 37 publications

Actin and CDC-42 contribute to nuclear migration through constricted spaces in C. elegans

Actin and CDC-42 contribute to nuclear migration through constricted spaces in C. elegans

Subcellular patterns of SPE-6 localization reveal unexpected complexities inCaenorhabditis eleganssperm activation and sperm function

E3 ubiquitin ligase Mindbomb 1 facilitates nuclear delivery of adenovirus genomes

Contact Info

Product

Resources

About