IndraLab

Statements

P97 binds YOD1. 13 / 13
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"In aggregate, YOD1 interacts directly with p97 and is a novel constituent of the ER dislocation machinery, thereby placing it in a perfect position to process ubiquitinated dislocation substrates in association with p97."
19818707
sparser
"YOD1, the mammalian homolog of Otu1, also interacts with p97 through its UBX domain [ xref ]."
28159894
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"Overexpression of SCF FBXO27 promotes K48-linked ubiquitylation of LAMP2 and to a lesser extent LAMP1 [ xref ], but whether this E3 ligase is responsible for assembly of K48-linked chains that are removed by p97-YOD1 is unknown ( xref )."
36713230
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"To confirm that p97 and YOD1 form a complex in a cellular context, we transfected FLAG-tagged YOD1 variants, followed by preparation of detergent extracts."
19818707
sparser
"In addition, we confirmed binding of recombinant YOD1 to p97 by GST-PD ( xref )."
28244869
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"In addition, p97 binds to a deubiquitinating enzyme YOD1, presumably so that polyubiquitin chains will not interfere with insertion into the proteasome ( xref )."
25071743
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"YOD1 interacts with p97 via its UBX domain."
21468305
sparser
"We showed that p97 associates with YOD1 by virtue of its UBX domain and that YOD1 participates in a p97 complex that also contains NPL4 and UFD1 ( xref and xref ), involved in the dislocation of misfolded proteins from the ER (Ye et al., xref , xref )."
19818707
sparser
"Importantly, a deletion variant of YOD1 (ΔUBX-GFP YOD1) that does not bind p97 still co-precipitated UBXD8 ( xref )."
19818707
sparser
"The UBX-like domain of OTUD2 binds AAA+ ATPase p97, an important Ub-dependent regulator of protein homeostasis ( xref )."
27066941
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"YOD1 is associated with p97 to facilitate protein dislocation, in which the 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 [ xref ]."
37667382
sparser
"In mammalian cells the deubiquitylating enzyme YOD1 binds to the p97 complex [117] ."
20599420
sparser
"Yod1 , which is specifically associated with macro-autophagy, and codes for the cofactor YOD1, which binds with p97 to promote lysosomal clearance ( xref ), was significantly increased in the FMD 3xTg male cohort compared with male 3xTg controls, although this effect was not observed in female 3xTg mice ( xref ; xref , page 47)."
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