Ignet

Gene Information

Gene symbol: DERL1

Gene name: derlin 1

HGNC ID: 28454

Synonyms: MGC3067, PRO2577, FLJ13784, DER1, DER-1, derlin-1

Related Genes

#	Gene Symbol	Number of hits
1	AVPR2	1 hits
2	RPS27A	1 hits
3	TM9SF1	1 hits
4	VCP	1 hits

Related Sentences

#	PMID	Sentence
1	16186510	Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.
2	16186510	In higher eukaryotes, p97 is bound to the ER membrane by a membrane protein complex containing Derlin-1 and VCP-interacting membrane protein (VIMP).
3	16186510	Here, we report that p97 interacts directly with several ubiquitin ligases and facilitates their recruitment to Derlin-1.
4	16186510	During retrotranslocation, a substrate first interacts with Derlin-1 before p97 and other factors join the complex.
5	16186510	These data, together with the fact that Derlin-1 is a multispanning membrane protein forming homo-oligomers, support the idea that Derlin-1 is part of a retrotranslocation channel that is associated with both the polyubiquitination and p97-ATPase machineries.
6	16186510	Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.
7	16186510	In higher eukaryotes, p97 is bound to the ER membrane by a membrane protein complex containing Derlin-1 and VCP-interacting membrane protein (VIMP).
8	16186510	Here, we report that p97 interacts directly with several ubiquitin ligases and facilitates their recruitment to Derlin-1.
9	16186510	During retrotranslocation, a substrate first interacts with Derlin-1 before p97 and other factors join the complex.
10	16186510	These data, together with the fact that Derlin-1 is a multispanning membrane protein forming homo-oligomers, support the idea that Derlin-1 is part of a retrotranslocation channel that is associated with both the polyubiquitination and p97-ATPase machineries.
11	16186510	Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.
12	16186510	In higher eukaryotes, p97 is bound to the ER membrane by a membrane protein complex containing Derlin-1 and VCP-interacting membrane protein (VIMP).
13	16186510	Here, we report that p97 interacts directly with several ubiquitin ligases and facilitates their recruitment to Derlin-1.
14	16186510	During retrotranslocation, a substrate first interacts with Derlin-1 before p97 and other factors join the complex.
15	16186510	These data, together with the fact that Derlin-1 is a multispanning membrane protein forming homo-oligomers, support the idea that Derlin-1 is part of a retrotranslocation channel that is associated with both the polyubiquitination and p97-ATPase machineries.
16	16186510	Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.
17	16186510	In higher eukaryotes, p97 is bound to the ER membrane by a membrane protein complex containing Derlin-1 and VCP-interacting membrane protein (VIMP).
18	16186510	Here, we report that p97 interacts directly with several ubiquitin ligases and facilitates their recruitment to Derlin-1.
19	16186510	During retrotranslocation, a substrate first interacts with Derlin-1 before p97 and other factors join the complex.
20	16186510	These data, together with the fact that Derlin-1 is a multispanning membrane protein forming homo-oligomers, support the idea that Derlin-1 is part of a retrotranslocation channel that is associated with both the polyubiquitination and p97-ATPase machineries.
21	18048502	Derlin-1 and p97/valosin-containing protein mediate the endoplasmic reticulum-associated degradation of human V2 vasopressin receptors.
22	18048502	Among them is X-linked nephrogenic diabetes insipidus, caused by mutations in the gene encoding the V2 vasopressin receptor (V2R).
23	18048502	Here, we show for the first time that V2R mutants with different misfolded domains are able to coprecipitate the ERAD components p97/valosin-containing protein, Derlin-1 and the 26S proteasome regulatory subunit 7.
24	18048502	Our results demonstrate the presence of a Derlin-1-mediated ERAD pathway degrading wild-type and disease-causing V2R mutants with different misfolded domains in a mammalian system.
25	18048502	Derlin-1 and p97/valosin-containing protein mediate the endoplasmic reticulum-associated degradation of human V2 vasopressin receptors.
26	18048502	Among them is X-linked nephrogenic diabetes insipidus, caused by mutations in the gene encoding the V2 vasopressin receptor (V2R).
27	18048502	Here, we show for the first time that V2R mutants with different misfolded domains are able to coprecipitate the ERAD components p97/valosin-containing protein, Derlin-1 and the 26S proteasome regulatory subunit 7.
28	18048502	Our results demonstrate the presence of a Derlin-1-mediated ERAD pathway degrading wild-type and disease-causing V2R mutants with different misfolded domains in a mammalian system.
29	18048502	Derlin-1 and p97/valosin-containing protein mediate the endoplasmic reticulum-associated degradation of human V2 vasopressin receptors.
30	18048502	Among them is X-linked nephrogenic diabetes insipidus, caused by mutations in the gene encoding the V2 vasopressin receptor (V2R).
31	18048502	Here, we show for the first time that V2R mutants with different misfolded domains are able to coprecipitate the ERAD components p97/valosin-containing protein, Derlin-1 and the 26S proteasome regulatory subunit 7.
32	18048502	Our results demonstrate the presence of a Derlin-1-mediated ERAD pathway degrading wild-type and disease-causing V2R mutants with different misfolded domains in a mammalian system.