Search bioRxiv⌕ Search

Biology subjects

Mengistu, D. Y.

Publications and source records attributed to Mengistu, D. Y..

2 recordsLinked to original sources

Distinct Cellular Effects of Myotonic Dystrophy type 2 RAN Tetrapeptides in Drosophila melanogaster

Myotonic dystrophy type 2 (DM2) is an autosomal dominant, multisystemic disorder caused by the expansion of CCTG repeats in the first intron of the CNBP gene. Repeat-associated non-AUG (RAN) translation of the expanded CCTG RNA may produce two tetrapeptide repeat proteins (TPRs), poly-QAGR and poly-PACL, whose roles in DM2 pathogenesis remain poorly understood. To investigate their individual contributions, we expressed codon-optimized QAGR and PACL peptides with ATG start codon in Drosophila melanogaster. Expression of QAGR and PACL TPRs significantly compromised fly viability and lifespan, induces eye degeneration and locomotor defects. We found that QAGR accumulated in the nucleolus, disrupted nucleolar integrity, and compromised rRNA processing. Moreover, QAGR expression interfered with autophagy, leading to the accumulation of Atg8a- and Ref(2)P-positive aggregates. Genetic interaction studies showed that overexpression of Atg8a or Ref(2)P mitigated QAGR-induced eye-toxicity, while knockdown of autophagy genes exacerbated it. Conversely, PACL repeats promoted stress granule formation, as indicated by their colocalization with TIAR in human cells and their epistatic interaction with the Drosophila orthologue Rox8. Notably, cytoplasmic PACL aggregates were observed in myoblasts of DM2 patient. Together these findings demonstrate that QAGR and PACL peptides exert distinct toxic effects, impairing nucleolar function and autophagy, or altering stress granule dynamics, respectively. Both mechanisms likely converge to drive DM2 pathogenesis and represent promising therapeutic targets.

genetics↗

Microcephaly-Associated Genes asp and Sas4 Control Chromatin Organization and Nuclear Lamina Structure in Drosophila melanogaster

Autosomal recessive primary microcephaly (MCPH) is a neurodevelopmental disorder characterized by reduced brain size and non-progressive intellectual disability. Mutations in over 30 genes have been linked to MCPH. Nearly a half of the genes identified by these mutations encode proteins involved in centrosome biogenesis or microtubule (MT) dynamics, suggesting a central role for mitotic spindle organization and division plane orientation in disease aetiology. However, it has been suggested that disruptions in spindle positioning alone are not sufficient to lead to microcephaly. Here, we investigate the contribution of the Drosophila orthologs of ASPM/MCPH5 (asp) and CENPJ/MCPH6 (Sas4) to nuclear architecture, chromatin organization, and genome stability. We show that loss of either Sas4 or Asp leads to aberrant microtubule architecture, mislocalization of the LINC complex, and deformation of the nuclear lamina. These defects are accompanied by reduced levels of both lamin and HP1 and impaired centromere clustering in interphase cells. Sas4 and asp mutants also exhibit a global reduction in heterochromatin-associated histone marks (H3K9me2/3 and H3K27me3) and increased levels of the euchromatin-associated mark H3K4me3. Remarkably, treatment with Methylstat, a demethylase inhibitor, reduced nuclear invaginations by partially restoring H3K9me3 levels. Additionally, Sas4 or Asp depletion leads to DNA damage, increased sensitivity to genotoxic stress, and delayed DNA repair. Together, these findings reveal a previously underappreciated role for Asp and Sas4 in preserving nuclear architecture and chromatin integrity, offering new insight into the pathogenesis of MCPH. GRAPHICAL ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=140 SRC="FIGDIR/small/666102v1_ufig1.gif" ALT="Figure 1"> View larger version (79K): org.highwire.dtl.DTLVardef@bfdfbborg.highwire.dtl.DTLVardef@f983eaorg.highwire.dtl.DTLVardef@143857borg.highwire.dtl.DTLVardef@1f0895b_HPS_FORMAT_FIGEXP M_FIG C_FIG

genetics↗