TL;DR: Parl-associated rhomboid-like (PARL-like) as mentioned in this paper is an inner mitochondrial membrane rhomboids of unknown function, whose yeast ortholog is involved in mitochondrial fusion.
TL;DR: It is demonstrated that rhomboid (Rho)- and Star-mediated activation of EGFR and ERK signaling increases sleep in a dose-dependent manner, and that blockade of rho expression in the nervous system decreases sleep.
Abstract: Epidermal growth factor receptor (EGFR) signaling in the mammalian hypothalamus is important in the circadian regulation of activity. We have examined the role of this pathway in the regulation of sleep in Drosophila melanogaster. Our results demonstrate that rhomboid (Rho)- and Star-mediated activation of EGFR and ERK signaling increases sleep in a dose-dependent manner, and that blockade of rhomboid (rho) expression in the nervous system decreases sleep. The requirement of rho for sleep localized to the pars intercerebralis, a part of the fly brain that is developmentally and functionally analogous to the hypothalamus in vertebrates. These results suggest that sleep and its regulation by EGFR signaling may be ancestral to insects and mammals.
TL;DR: In this article, an error in the gene ID for TimRhom I, cited in the Methods, which specified an unrelated gene, was corrected in both the PDF and HTML versions of the article.
Abstract: Nature Communications 7: Article number:13707 (2016); Published: 19 December 2016; Updated: 30 June 2017 The original version of this Article contained an error in the gene ID for TimRhom I, cited in the Methods, which specified an unrelated gene. The correct gene ID for TimRhom I is Tb927.9.8260. This has now been corrected in both the PDF and HTML versions of the Article.
TL;DR: It is proposed that substrate interaction and p97/VCP recruitment are separate functions that are essential for dislocation and can be assigned respectively to the rhomboid domain and the C terminus of Derlin-1 and that intramembrane proteolysis and protein dislocation share unexpected mechanistic features.
Abstract: Endoplasmic reticulum-associated degradation (ERAD) substrates must be dislocated across the ER membrane through a process driven by the ATPase p97/VCP, and Derlins are thought to be part of the dislocation machinery. New data identify Derlin-1 as an inactive member of the rhomboid family that facilitates the release of ERAD substrates from the ER, following their transfer across the membrane.
TL;DR: The evolutionary conserved rhomboid family protein RHBDL4 is a ubiquitin-dependent ER-resident intramembrane protease that is upregulated upon ER stress and specifically binds the AAA+-ATPase p97, suggesting that proteolytic processing and dislocation into the cytosol are functionally linked.