
Frontiers | Gp78 E3 Ubiquitin Ligase: Essential Functions and ...
2017年8月24日 · Glycoprotein 78 (Gp78) is an E3 ubiquitin ligase that prevents multifactorial deleterious accumulation of different misfolded proteins via endoplasmic reticulum-associated degradation (ERAD). However, the precise role of Gp78 under stress conditions to avoid bulk misfolded aggregation is unclear, which can act as a crucial resource to establish ...
Gp78, an E3 ubiquitin ligase acts as a gatekeeper suppressing
2015年3月19日 · Gp78 is E3 ligase, which regulates endoplasmic reticulum-associated degradation (ERAD) by ubiquitinylation of misfolded ER proteins. Here, we report that upon ageing (12 months), gp78-/- mice developed obesity, recapitulating age-related human NASH.
Regulation of mitophagy by the Gp78 E3 ubiquitin ligase
Glycoprotein 78 (Gp78) is a critical E3 ubiquitin ligase in endoplasmic reticulum-associated degradation. Overexpression of Flag-tagged Gp78 (Flag-gp78), but not Flag-gp78 mutated in its RING-finger domain (Flag-RINGmut) with deficient ubiquitin ligase activity, induces mitochondrial fragmentation a …
Gp78 E3泛素连接酶:蛋白质稳态的基本功能和 ... - X-MOL
2017年9月12日 · 糖蛋白78(Gp78)是一种E3泛素连接酶,可通过内质网相关降解(ERAD)防止不同折叠错误的蛋白质的多因素有害积累。但是,尚不清楚在应激条件下Gp78在避免大量错误折叠的聚集中的确切作用,它可以作为建立蛋白质组动态性质的关键资源。
Gp78, a Membrane-Anchored Ubiquitin Ligase, Associates
2005年9月16日 · Here, we show that gp78, a membrane bound E3, binds to Insig-1 and is required for sterol-regulated ubiquitination of reductase. In addition, gp78 couples regulated ubiquitination to degradation of reductase by binding to VCP, an ATPase that plays a key role in recognition and degradation of ERAD substrates.
Regulation of mitophagy by the Gp78 E3 ubiquitin ligase
2013年4月4日 · The Gp78 E3 ubiquitin ligase is shown to target the mitofusin mitochondrial fusion proteins for degradation, inducing mitochondrial fission and mitofusin 1–dependent mitophagy of uncoupled mitochondria. Mitophagy induced by endoplasmic reticulum–associated gp78 defines a distinct cellular pathway to eliminate damaged mitochondria.
p38 MAP kinase–dependent phosphorylation of the Gp78 E3 …
2015年11月1日 · Gp78 is an ERAD-associated E3 ubiquitin ligase that induces degradation of the mitofusin mitochondrial fusion proteins and mitochondrial fission. Gp78 is localized throughout the ER; however, the anti-Gp78 3F3A monoclonal antibody (mAb) recognizes Gp78 selectively in mitochondria-associated ER domains.
The activity of a human endoplasmic reticulum-associated degradation E3 ...
2006年1月3日 · In this study, we establish that a human ubiquitin ligase (E3), gp78, and a specific E2, Ube2g2, are both critically important for ERAD of multiple substrates. gp78 exhibits a complex domain structure that, in addition to the RING finger, includes a ubiquitin-binding Cue domain and a specific binding site for Ube2g2.
Gp78 E3 Ubiquitin Ligase: Essential Functions and ... - PubMed
2017年8月25日 · Glycoprotein 78 (Gp78) is an E3 ubiquitin ligase that prevents multifactorial deleterious accumulation of different misfolded proteins via endoplasmic reticulum-associated degradation (ERAD). However, the precise role of Gp78 under stress conditions to avoid bulk misfolded aggregation is unclear, which can act as a crucial resource to establish ...
RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ...
2012年7月30日 · Gp78 is an E3 ubiquitin ligase within the endoplasmic reticulum-associated degradation pathway. We show that Flag-tagged gp78 undergoes sulfhydryl cysteine palmitoylation (S-palmitoylation) within the RING finger motif, responsible for …
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