TY  - GEN
T1  - Mutations in two ERAD E3 ubiquitin ligase enzymes reduce spontaneous reversal frequency in Caenorhabditis elegans
AU  - Oswald, Mackenzi
AU  - Hulsey-Vincent, Heino
AU  - Dahlberg, Caroline (Lina)
DO  - 10.17912/micropub.biology.000329
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000329/
AB  - Secretory and membrane-bound proteins must be properly folded and matured at the endoplasmic reticulum (ER). Despite the molecular machinery dedicated to these processes, up to 1/3 of proteins are destroyed within minutes of their synthesis (Hirsch et al. 2009; Schubert et al. 2000). Misfolded proteins in the endoplasmic reticulum can accumulate and disrupt proteostasis, which can contribute to neurodegenerative diseases. The Endoplasmic Reticulum Associated Degradation (ERAD) pathway relies on E2 ubiquitin-conjugating enzymes and E3 ubiquitin ligases to ubiquitylate misfolded proteins, signaling for degradation of these misfolded proteins by the proteasome (Vembar and Brodsky 2008). Three putative E3 ligases that are expected to be involved in ERAD in C. elegans are HRDL-1, HRD-1, and MARC-6 (Sasagawa et al. 2007). We used strains harboring mutations in hrdl-1, hrd-1 and marc-6 genes to determine if these proteins are required for regulating spontaneous reversal behavior in C. elegans.
PY  - 2020
JO  - microPublication Biology
ER  -