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PMID:19818707

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Citation

Ernst, R, Mueller, B, Ploegh, HL and Schlieker, C (2009) The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol. Cell 36:28-38

Abstract

YOD1 is a highly conserved deubiquitinating enzyme of the ovarian tumor (otubain) family, whose function has yet to be assigned in mammalian cells. YOD1 is a constituent of a multiprotein complex with p97 as its nucleus, suggesting a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. Expression of a YOD1 variant deprived of its deubiquitinating activity imposes a halt on the dislocation reaction, as judged by the stabilization of various dislocation substrates. Accordingly, we observe an increase in polyubiquitinated dislocation intermediates in association with p97 in the cytosol. This dominant-negative effect is dependent on the UBX and Zinc finger domains, appended to the N and C terminus of the catalytic otubain core domain, respectively. The assignment of a p97-associated ubiquitin processing function to YOD1 adds to our understanding of p97's role in the dislocation process.

Links

PubMed PMC2774717 Online version:10.1016/j.molcel.2009.09.016

Keywords

Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Carrier Proteins/metabolism; Catalytic Domain/physiology; Cell Cycle Proteins/genetics; Cell Cycle Proteins/metabolism; Cell Line; Endopeptidases/physiology; Endoplasmic Reticulum/metabolism; Humans; Membrane Proteins/genetics; Membrane Proteins/metabolism; Point Mutation/physiology; Proteasome Endopeptidase Complex/metabolism; Protein Binding/physiology; Protein Folding; Protein Interaction Domains and Motifs/physiology; Protein Transport/physiology; Receptors, Antigen, T-Cell, alpha-beta/genetics; Receptors, Antigen, T-Cell, alpha-beta/metabolism; Thiolester Hydrolases/physiology; Transfection; Ubiquitin/metabolism; Ubiquitination/genetics; Zinc Fingers/physiology; alpha 1-Antitrypsin/genetics; alpha 1-Antitrypsin/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:TERA

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q5VVQ6

F

Seeded From UniProt

complete

HUMAN:OTU1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55072

F

Seeded From UniProt

complete

HUMAN:OTU1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9BUN8

F

Seeded From UniProt

complete

HUMAN:OTU1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q96CS3

F

Seeded From UniProt

complete

HUMAN:OTU1

involved_in

GO:0030968: endoplasmic reticulum unfolded protein response

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:OTU1

involved_in

GO:0030433: ubiquitin-dependent ERAD pathway

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:OTU1

enables

GO:0004843: thiol-dependent deubiquitinase

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:OTU1

involved_in

GO:0071108: protein K48-linked deubiquitination

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:OTU1

involved_in

GO:0070536: protein K63-linked deubiquitination

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:FAF2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q5VVQ6

F

Seeded From UniProt

complete

HUMAN:DERL1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q5VVQ6

F

Seeded From UniProt

complete


See also

References

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