Disease relevance of Sec61alpha

• Loss-of-function experiments for DSec61alpha revealed that the translocon contributes to expanded polyglutamine-mediated neuronal toxicity, likely resulting from proteasome inhibition and leading to accumulation of ubiquitinated proteins [1].

High impact information on Sec61alpha

• Taken together, proteasome inhibition by expanded polyglutamine tracts may lead to the accumulation of toxic undegraded proteins normally transported by the Sec61alpha translocon [1].
• To elucidate mechanisms in neural cell death and degeneration, we characterized the Drosophila ortholog of Sec61alpha (DSec61alpha), a component of the translocon that is involved in both protein import and endoplasmic reticulum-associated degradation [1].
• Cytosol-endoplasmic reticulum interplay by Sec61alpha translocon in polyglutamine-mediated neurotoxicity in Drosophila [1].
• Of these, we identified and characterized the endd2 gene, which encodes the Drosophila ortholog of Sec61alpha (DSec61alpha), an endoplasmic reticulum protein with protein translocation activity [2].

References