IndraLab

Statements

USP37 is phosphorylated. 22 / 22
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"CDK2 regulates ERK1/2 stability by phosphorylating and activating USP37."
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sparser
"A detailed structural analysis of phosphorylated USP37 may be required to reveal this mechanism."
34177595
sparser
"CDK1/2 inhibitors, but not CDK4/6 inhibitors, inhibited USP37 phosphorylation ( xref )."
37955924
sparser
"As shown in xref , the S628A mutant of USP37 markedly decreased phospho-CDK substrate signaling, suggesting that S628 is a major site for CDK1/2 mediation of USP37 phosphorylation."
37955924
sparser
"We found this interesting because USP37 has been implicated in cell proliferation and transformation [ 6, 7 ] as well as in cell-cycle regulation, where during the G1/S transition, CDK2 phosphorylates[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26299517
sparser
"However, USP37 phosphorylation did not affect its binding to ERK1/2 ( xref )."
37955924
sparser
"These findings suggest that the CDK2-mediated phosphorylation of USP37 exerted a vital function in regulating USP37 DUB activity and the USP37-mediated deubiquitination and stabilization of ERK1/2."
37955924
sparser
"Meanwhile, USP37 is phosphorylated and activated by CDK2, promoting the removal of polyubiquitin chains from ERK1/2 and resulting in the stabilization of ERK1/2."
37955924
rlimsp
"We observed that just as CDC6, the levels of USP37 protein and phosphorylated USP37 decreased in the presence of CDK2 inhibitor ( )."
25347529
sparser
"Subsequent phosphorylation of USP37 by either CDK2/cyclin E or CDK2/cyclin A triggers its full DUB activity."
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rlimsp
"Plk1-mediated phosphorylation of USP37 plays an important role in its recognition by SCF-β-TrCP [7]."
25347529
sparser
"Inactivation of CDK2 in mitosis results in loss of USP37 phosphorylation."
21596315
sparser
"Therefore USP37 phosphorylation correlated with its cell cycle-specific DUB activity."
21596315
sparser
"Finally, recombinant CDK2/cyclin A phosphorylated wild-type USP37, but neither USP37-S 628 A nor USP37-S 628 D, in an in vitro kinase assay ( Figure 7 H)."
21596315
sparser
"Collectively, these data identify CDK2 as the kinase responsible for phosphorylating and activating USP37 during G1/S. We show that USP37 is a DUB that associates with and antagonizes APC CDH1 follow[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
21596315
sparser
"Therefore USP37 phosphorylation, like RB, is a marker for the G1/S transition."
21596315
sparser
"We think that USP37, which is itself an APC CDH1 substrate ( Figure 5 ), is stable during S and G2 for two reasons: (1) phosphorylated USP37 deubiquitinates itself, and (2) CDH1 is phosphorylated by [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
21596315
sparser
"Another possibility is that phosphorylated USP37 recruits cofactors that increase its DUB activity."
21596315
sparser
"Next, we investigated whether USP37 phosphorylation affects its ability to remove ubiquitination of SAMHD1."
39655951
sparser
"Therefore, the phosphorylation of USP37 does not affect its deubiquitination activity toward SAMHD1."
39655951
sparser
"Furthermore, phosphorylation of USP37 is a cell cycle-dependent event."
34177595
rlimsp
"Further, inhibition of CDK2 activity in HBx expressing cells, resulted in a decrease of not only phosphorylated USP37 but also total USP37 protein levels."
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