Pro178 and Pro183 of Selenoprotein S Are Essential Residues for Interaction with p97(VCP) during Endoplasmic Reticulum-associated Degradation

Lee, Jea Hwang; Kwon, Joon Hyun; Jeon, Yeong Ha; Ko, Kwan Young; Lee, Seung Rock; Kim, Ick Young

doi:10.1074/jbc.m113.534529

Cited by 45 publications

(75 citation statements)

References 57 publications

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“…CD3␦ has been known as a substrate for Hrd1-and gp78-mediated ERAD (14,20). We also found that CD3␦ was the substrate for SelS-mediated ERAD (12). SelS, which is also known as VCP-interacting membrane protein, is a selenoprotein that contains a single selenocysteine (Sec, U) at position 188, which is the penultimate C-terminal residue (21)(22)(23).…”

mentioning

confidence: 85%

“…It has recently been demonstrated that, during ERAD, p97(VCP) forms a complex with derlins, SelS, and E3 liagases that plays an important role in the extraction of misfolded proteins from the ER to the cytosol (12,16,17). The association of p97(VCP) with derlins depends on the SelS.…”

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confidence: 99%

“…The interaction of p97(VCP) with its binding partners and co-factors plays a key role in its activity and subcellular location (10). When p97(VCP) is relocalized to the ER membrane via its interaction with its binding partners, such as SelS, gp78, and Hrd1 (7,(12)(13)(14), it has an essential function in the maintenance of ER homeostasis and the regulation of ER stress through ERAD (15).…”

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confidence: 99%

“…gp78 and SelS recruit p97(VCP) to the ER membrane, which mediates the ERAD machinery. Both gp78 and SelS have the VCP-interacting motif (VIM) (12,13). gp78 needs the VIM for interaction with p97(VCP) (13), whereas SelS does not require the VIM to recruit p97(VCP) to the ER membrane (12).…”

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confidence: 99%

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Selenoprotein S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated Degradation

Lee

Park

Jang

et al. 2015

Journal of Biological Chemistry

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Cytosolic valosin-containing protein (p97(VCP)) is translocated to the ER membrane by binding to selenoprotein S (SelS), which is an ER membrane protein, during endoplasmic reticulum-associated degradation (ERAD). Selenoprotein K (SelK) is another known p97(VCP)-binding selenoprotein, and the expression of both SelS and SelK is increased under ER stress. To understand the regulatory mechanisms of SelS, SelK, and p97(VCP) during ERAD, the interaction of the selenoproteins with p97(VCP) was investigated using N2a cells and HEK293 cells. Both SelS and SelK co-precipitated with p97(VCP). However, the association between SelS and SelK did not occur in the absence of p97(VCP). SelS had the ability to recruit p97(VCP) to the ER membrane but SelK did not. The interaction betweenSelK and p97(VCP) did not occur in SelS knockdown cells, whereas SelS interacted with p97(VCP) in the presence or absence of SelK. These results suggest that p97(VCP) is first translocated to the ER membrane via its interaction with SelS, and then SelK associates with the complex on the ER membrane. Therefore, the interaction between SelK and p97(VCP) is SelSdependent, and the resulting ERAD complex (SelS-p97(VCP)-SelK) plays an important role in ERAD and ER stress.

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confidence: 85%

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Selenoprotein S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated Degradation

Lee

Park

Jang

et al. 2015

Journal of Biological Chemistry

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“…This domain neither displays structural similarity to any of the known p97 interacting domains nor does it contain any of the linear binding motifs. Other examples are the CSN5 subunit of the COP9 signalosome, which is proposed to interact via its MPN domain with the N domain [99] or SelS/VIMP, which instead of using its VIM binds via two proline residues [100].…”

Section: Non-canonical Binding Domains/motifsmentioning

confidence: 99%

Control of p97 function by cofactor binding

2015

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Edited by Wilhelm JustKeywords: ATPases Associated with diverse cellular Activities p47 UFD1-NPL4 UBXD1 Inclusion Body Myopathy with Pagets disease of the bone and Fronto-temporal Dementia a b s t r a c t p97 (also known as Cdc48, Ter94, and VCP) is an essential, abundant and highly conserved ATPase driving the turnover of ubiquitylated proteins in eukaryotes. Even though p97 is involved in highly diverse cellular pathways and processes, it exhibits hardly any substrate specificity on its own. Instead, it relies on a large number of regulatory cofactors controlling substrate specificity and turnover. The complexity as well as temporal and spatial regulation of the interactions between p97 and its cofactors is only beginning to be understood at the molecular level. Here, we give an overview on the structural framework of p97 interactions with its cofactors, the emerging principles underlying the assembly of complexes with different cofactors, and the pathogenic effects of disease-associated p97 mutations on cofactor binding.

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Selenoprotein S Is Highly Expressed in the Blood Vessels and Prevents Vascular Smooth Muscle Cells From Apoptosis

et al. 2015

J of Cellular Biochemistry

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Atherosclerosis and related cardiovascular diseases (CVD) represent one of the greatest threats to human health worldwide. The protection of vascular smooth muscle cells (VSMCs) from apoptosis in the plaque has become an important therapeutic target for atherosclerotic plaque stabilization. A significant association of selenoprotein S (SelS) gene polymorphism with atherosclerotic CVD has been reported in epidemiologic studies, but the underlying mechanism remains unknown. In this paper, SelS expression in the thoracic aorta and its role in the protection of VSMCs from apoptosis have been studied. Western blot analysis showed that SelS was highly expressed in rat thoracic aorta. SelS gene silence by small interference RNA (siRNA) rendered VSMCs more sensitive to hydrogen peroxide- or tunicamycin- induced injury and apoptosis, as determined by MTT assay, Hoechst staining, and annexin V/propidium iodide staining. SelS silence aggravated hydrogen peroxide-induced oxidative stress and phosphorylation of p38 MAPK and c-Jun N-terminal kinase (JNK) in VSMCs. Furthermore, SelS silence enhanced endoplasmic reticulum (ER) stress induced by hydrogen peroxide or tunicamycin, as showed by the increased protein levels of ER chaperone 78 kDa glucose-regulated protein (GRP78), ER stress transducer phosphorylated protein kinase RNA like ER kinase (PERK), and the proapoptotic transcription factor C/EBP homologous protein (CHOP). In conclusion, the present study suggested that SelS highly expressed in the blood vessel might protect VSMCs from apoptosis by inhibiting oxidative stress and ER stress. Our finding provided mechanistic insights for the potential preventive role of SelS in atherosclerotic CVD.

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Pro178 and Pro183 of Selenoprotein S Are Essential Residues for Interaction with p97(VCP) during Endoplasmic Reticulum-associated Degradation

Cited by 45 publications

References 57 publications

Selenoprotein S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated Degradation

Selenoprotein S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated Degradation

Control of p97 function by cofactor binding

Selenoprotein S Is Highly Expressed in the Blood Vessels and Prevents Vascular Smooth Muscle Cells From Apoptosis

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