IndraLab

Statements

USP1 is phosphorylated on S313. 47 / 47
9 | 17 21
hprd
No evidence text available
18669648
rlimsp
"Another reversible modification of USP1 is phosphorylation at Ser313 by cyclin-dependent kinases (CDKs) [84]. Two functional consequences of Ser313 phosphorylation have been reported. On one hand, phosphorylation of this residue, which is located within USP1 degron motif (Figure 2), may contribute to regulate the cell-cycle dependent levels of USP1, by preventing its degradation in mitosis [84]."
23937906
hprd
No evidence text available
20068231
hprd
No evidence text available
19413330
rlimsp
"It has been recently reported that phosphorylation of USP1 at S313 is necessary for the interaction of this DUB with its cofactor UAF1 [17]."
25744535
rlimsp
"The pSer313-dependent formation of the USP1/UAF1 complex points to a new approach for inhibiting USP1 activity by disrupting the interaction between the UAF1's WD40-repeat domain and the Ser313-containing phosphopeptide in USP1."
23116119
rlimsp
"These include the role of the serine 313 phosphorylation site, the relative contribution of different USP1 sequence motifs to UAF1 binding, and the potential effect of cancer-associated mutations on USP1 regulation by autocleavage."
25744535
hprd
No evidence text available
20068231
sparser
"Our finding that phosphorylation of USP1 at S313 is dispensable for UAF1 binding in cells, led us to use the relocation assay to directly compare the relative contribution of two proposed UAF1-binding sites in USP1: the 235–408 fragment containing the S313 residue [ xref ], and the 420–520 fragment [ xref ]."
25744535
rlimsp
"The position of the diglycine motif (Gly-Gly), which constitutes the site of USP1 autocleavage, and the residue Ser313, which is the site of Cdk-mediated USP1 phosphorylation, are also indicated."
23937906
hprd
No evidence text available
19413330
sparser
"Our findings are in accord with previous proteomic analyses showing that Ser67 and Ser313 of USP1 were phosphorylated in human cells( xref , xref )."
23116119
rlimsp
"The location of USP1 nuclear localization signals (NLSs, in red), and the S313 phosphorylation site is also shown."
25744535
sparser
"It has been recently reported that phosphorylation of USP1 at S313 is necessary for the interaction of this DUB with its cofactor UAF1 [ xref ]."
25744535
sparser
"In contrast to previous in vitro findings, or results indicate that USP1 phosphorylation at S313 is not critical for PCNA deubiquitination, neither for binding to UAF1 in a cellular environment."
25744535
rlimsp
"In this study, we show that Ser313 phosphorylation in USP1 is required for its interaction with UAF1 and for the stimulation of USP1's activity."
23116119
sparser
"Phosphorylation of Ser313 in USP1 has been shown to be required for its proper interaction with UAF1( xref )."
23797609
rlimsp
"It has been recently reported that phosphorylation of USP1 at S313 is necessary for the interaction of this DUB with its cofactor UAF1 [17]. Since only in vitro evidence for S313 phosphorylation-regulated USP1/UAF1 interaction has been provided, we decided to evaluate the role that this phosphorylation site may have in regulating USP1 binding to UAF1 in a cellular context."
25744535
rlimsp
"Our results indicate that the S313 phosphorylation site is not critical for USP1 binding to UAF1 or for PCNA deubiquitination in a cellular environment."
25744535
rlimsp
"In this study, we show that Ser313 phosphorylation in USP1 is required for its interaction with UAF1 and for the stimulation of USP1's activity. In contrast, two other known USP1 serine phosphorylations (Ser42 and Ser67) are dispensable with respect to the activity of the USP1/UAF1 complex. An S313D phosphomimetic mutation in USP1 can substitute for Ser313 phosphorylation in promoting the formation of the USP1/UAF1 complex."
23116119
rlimsp
"In contrast, using cell-based assays, we have mapped the UAF1-binding region in USP1 to a 100 amino acid motif comprising residues 420–520, which does not include the S313 phosphorylation site [18]."
25744535
sparser
"USP1 phosphorylation at S313 is not critical for PCNA deubiquitination, neither for binding to UAF1 in a cellular environment."
25744535
hprd
No evidence text available
20068231
sparser
"The interaction with UAF1 is regulated by USP1 phosphorylation at Ser313 [ xref , xref , xref ]."
32512887
sparser
"To confirm that the interaction between USP1 and UAF1 is mediated by USP1 Ser313 phosphorylation, six-His-tagged USP1 was coexpressed with untagged UAF1 in insect cells."
23116119
hprd
No evidence text available
18669648
hprd
No evidence text available
18669648
rlimsp
"Conclusions: USP1 phosphorylation at S313 is not critical for PCNA deubiquitination, neither for binding to UAF1 in a cellular environment."
25744535
sparser
"The interaction with UAF1 is regulated by USP1 phosphorylation at Ser313 [ xref ]."
32512887
rlimsp
"In this study, we show that Ser313 phosphorylation in USP1 is required for its interaction with UAF1 and for the stimulation of USP1's activity. In contrast, two other known USP1 serine phosphorylations (Ser42 and Ser67) are dispensable with respect to the activity of the USP1/UAF1 complex. An S313D phosphomimetic mutation in USP1 can substitute for Ser313 phosphorylation in promoting the formation of the USP1/UAF1 complex. We further demonstrated that CDK1 is responsible for Ser313 phosphorylation, and protein phosphatase treatment of USP1 can lead to inactivation of USP1/UAF1. An inserted domain in USP1 (amino acids 235-408) was found to interact with UAF1, and this interaction is mediated by Ser313 phosphorylation."
23116119
rlimsp
"Structure-function analysis of USP1: insights into the role of Ser313 phosphorylation site and the effect of cancer-associated mutations on autocleavage."
25744535
sparser
"Phosphorylation of USP1 on Ser313 can influence its interaction with the cofactor USP1-associated factor 1 (UAF1)."
34177595
sparser
"It will be of interest to assess the effect of USP1 Ser313 phosphorylation on its interaction with Cdh1."
23116119
rlimsp
"On the other hand, phosphorylation of Ser313 has been reported to be necessary for USP1 interaction with UAF1 in an in vitro experimental setting [74], thus raising the possibility that Ser313 phosphorylation could be a critical regulatory event for USP1 enzymatic activity, although these findings await further confirmation in a more physiological setting."
23937906
rlimsp
"In contrast, using cell-based assays, we have mapped the UAF1-binding region in USP1 to a 100 amino acid motif comprising residues 420–520, which does not include the S313 phosphorylation site [18]. It is, therefore, necessary to clarify these conflicting results, and to determine to what extent these two amino acid motifs, and the S313 phosphorylation site, contribute to USP1/UAF1 interaction."
25744535
sparser
"A previous study reported that CDK1 is responsible for phosphorylation of Ser313 of USP1 in human cells( xref )."
23116119
rlimsp
"Our finding that phosphorylation of USP1 at S313 is dispensable for UAF1 binding in cells, led us to use the relocation assay to directly compare the relative contribution of two proposed UAF1-binding sites in USP1: the 235–408 fragment containing the S313 residue [17], and the 420–520 fragment [18]."
25744535
rlimsp
"CONCLUSIONS: USP1 phosphorylation at S313 is not critical for PCNA deubiquitination, neither for binding to UAF1 in a cellular environment."
25744535
hprd
No evidence text available
19413330
rlimsp
"The finding that the non-phosphorylatable S313A mutant version of USP1 binds and is stabilized by UAF1 in our cell-based assays indicates that phosphorylation at S313 is not critical for USP1/UAF1 complex formation in a cellular context."
25744535
sparser
"It was suggested that phosphorylation of USP1 at Ser313 serves as an interface for the association of USP1 with UAF1."
23116119
sparser
"Remarkably, the stimulatory effect of USP1 Ser313 phosphorylation requires UAF1, a WD40-repeat protein that interacts with USP1."
23116119
sparser
"These results suggest that USP1 Ser313 phosphorylation is required for formation of the complex between USP1 and UAF1."
23116119
rlimsp
"In contrast to previous in vitro findings, or results indicate that USP1 phosphorylation at S313 is not critical for PCNA deubiquitination, neither for binding to UAF1 in a cellular environment."
25744535
sparser
"USP1 Ser313 phosphorylation promotes complex formation between USP1 and UAF1."
23116119
sparser
"In this study we show that Ser313 phosphorylation in USP1 is required for its interaction with UAF1 and for the stimulation of USP1’s activity."
23116119
rlimsp
"Thus, cyclin-dependent kinase 1 (CDK1)-mediated phosphorylation of S313 during M phase was shown to prolong the stability of USP1 presumably by preventing its degradation by the anaphase-promoting complex/cyclosome [16]."
25744535