IndraLab

Statements

YOD1 binds GEMIN4. 7 / 7
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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
reach
"The DUB YOD1, which binds to p97 via its UBX (ubiquitin regulatory X) domain, is also associated with ERAD [XREF_BIBR]."
28819009
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"We show that a catalytically inactive deubiquitinating enzyme and p97 cofactor YOD1 enhances the accumulation of K11- and K48 linked polyubiquitin in the cytoplasm, at the ER membrane, and bound to p97."
24417208
reach
"In addition, p97 binds to a deubiquitinating enzyme YOD1, presumably so that polyubiquitin chains will not interfere with insertion into the proteasome."
25071743
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"In addition, whereas both H. sapiens YOD1 and OTUD2 and S. cerevisiae Otu1 interact with p97 and Cdc48 through an N-terminal UBL or UBX domain, the A. thaliana OTU2 has a relatively shorter N-terminus and does not interact with CDC48."
24659992
reach
"yOtu1 and D.melanogaster (dm) Otu1 are orthologs of human OTUD2 (38% and 53% identical in OTU domain, respectively), and OTUD2 and yOtu1 both bind cdc48 and p97 and are involved in endoplasmic-reticulum-associated protein degradation."
23827681
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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