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- W41858034 abstract "The endoplasmic reticulum (ER)-associated degradation (ERAD) pathway is responsible for the degradation of aberrant proteins in the ER and the regulated degradation of several ER resident proteins. Inositol 1,4,5-trisphosphate receptors (IP3Rs) form tetrameric Ca2+ channels in the ER membrane and are converted from stable proteins into ERAD substrates following their activation by IP3 and Ca2+. Using activated, endogenous IP3Rs as a tool, we have recently identified two novel mediators of the mammalian ERAD pathway—SPFH1 and SPFH2 (SPFH domain-containing protein, members 1 and 2). SPFH1 and SPFH2 associate with IP3Rs immediately after their activation but prior to their polyubiquitination, and depletion of either SPFH1 or SPFH2 by RNAi inhibited the ERAD of IP3Rs and other mammalian ERAD substrates. SPFH1 and SPFH2, both ER membrane proteins that protrude into the ER lumen, were found to exist exclusively as an ∼1MDa complex by native PAGE, and TEM of purified, endogenous SPFH1/2 complex indicates that it assembles into ring-like structures. These results suggest that SPFH1 and SPFH2 form a high molecular weight, ring-shaped complex in the ER membrane that plays a key role in the early steps of mammalian ERAD pathway, perhaps as a factor involved in substrate recognition or retrotranslocation. Sources of funding: NIH, PhRMA Foundation" @default.
- W41858034 created "2016-06-24" @default.
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- W41858034 date "2008-03-01" @default.
- W41858034 modified "2023-10-11" @default.
- W41858034 title "SPFH1 and SPFH2 form a high molecular weight complex in the ER membrane that mediates the ER‐associated degradation of inositol 1,4,5‐trisphosphate receptors and other substrates in mammalian cells" @default.
- W41858034 doi "https://doi.org/10.1096/fasebj.22.1_supplement.605.5" @default.
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