Protein OS-9

Definition:

Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.

References:

[1]. Yan Wang, et al. OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum. J Biol Chem. 2007 Dec 14;282(50):36561-70. [Content Brief]

[2]. John C Christianson, et al. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol. 2008 Mar;10(3):272-82. [Content Brief]

[3]. Tadashi Satoh, et al. Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation. Mol Cell. 2010 Dec 22;40(6):905-16. [Content Brief]

[4]. Felicity Alcock, et al. Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins. J Mol Biol. 2009 Jan 30;385(4):1032-42. [Content Brief]

[5]. Nobuko Hosokawa, et al. Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem. 2009 Jun 19;284(25):17061-17068. [Content Brief]

[6]. Riccardo Bernasconi, et al. A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal. J Biol Chem. 2008 Jun 13;283(24):16446-54. [Content Brief]

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