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YBX1 binds OTUB1. 27 / 27
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"To further explore the role of U0126 in regulating YB-1 protein stability, we performed coimmunoprecipitation (co-IP) and found that the treatment with U0126 restored the interaction between YB-1 and OTUB1 (Fig. 4G), thereby reducing YB-1 ubiquitination modification (Fig. 4H) and proteasome degradation."
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"Also, the interaction between YB-1 and OTUB1 was diminished by high glucose treatment (Fig. 2D)."
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"We recently demonstrated that the ischemia-reperfusion injury can impair the homeostatic interaction of YB-1 and OTUB1, which results in YB-1 K48 polyubiquitination and subsequent proteasome degradation in renal tubular cells ( xref )."
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"To further explore the role of U0126 in regulating YB-1 protein stability, we performed coimmunoprecipitation (co-IP) and found that the treatment with U0126 restored the interaction between YB-1 and OTUB1 ( xref G ), thereby reducing YB-1 ubiquitination modification ( xref H ) and proteasome degradation."
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"Given the role of deubiquitinase OTUB1 in regulating the ubiquitination and stability of YB-1 in renal tubular cells ( xref ), we aimed to investigate these roles of OTUB1–YB-1 axis in regulation of DCM."
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"Co-IP results showed the homeostatic interaction of YB-1 and OTUB1 in cardiomyocytes, which are sensitive to diabetic microenvironment."
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"In accordance with our in vitro findings, U0126 could suppress the ERK phosphorylation, RSK phosphorylation, and subsequent YB-1 S102 phosphorylation, resulting in enhanced interaction between YB-1 and OTUB1 and preserved YB-1 protein expression in diabetic hearts."
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"In diabetic cardiomyopathy, OTUB1 interacts with YB-1 to stabilize the YB-1 protein, thereby exerting a protective effect [ xref ]."
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"Study in vitro and in vivo indicated that hyperglycaemia caused the phosphorylation of S102 site of YB-1 in cardiomyocytes, which weakened the interaction between YB-1 and OTUB1, thus promoting the degradation of YB-1 through ubiquitin-proteasome pathway, leading to aggravation of diabetes cardiomyopathy (Ref. xref )."
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"aPC preserved the interaction of YB-1 with the deubiquitinating enzyme otubain-1 and maintained expression of otubain-1, which was required to reduce K48-linked YB-1 ubiquitination and to stabilize the 50 kD form of YB-1 after renal IRI and tubular HR injury."
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"We demonstrate that ERK inhibition with U0126 also suppressed the phosphorylation of the downstream RSK and YB-1 (S102), which stabilized the interaction between YB-1 and otubain-1 and thereby preserved YB-1 protein expression in diabetic hearts."
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"We recently demonstrated that the ischemia-reperfusion injury can impair the homeostatic interaction of YB-1 and OTUB1, which results in YB-1 K48 polyubiquitination and subsequent proteasome degradation in renal tubular cells (10)."
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"Mechanistically, hyperglycemia impairs the homeostatic interaction between YB-1 and OTUB1, which results in enhanced YB-1 ubiquitination and subsequent proteasome degradation."
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"Mechanistically, hyperglycemia impairs the homeostatic interaction between YB-1 and OTUB1, which results in enhanced YB-1 ubiquitination and subsequent proteasome degradation."
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"Hyperglycemia induced the phosphorylation of YB-1 at S102, which diminishes the interaction between YB-1 and OTUB1."
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"Also, the interaction between YB-1 and OTUB1 was diminished by high glucose treatment ( xref D )."
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"Moreover, SL-0101 restored the interaction between YB-1 and OTUB1 ( xref F ) and consequently ameliorated the ubiquitination modification of YB-1 ( xref G )."
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"Hyperglycemia induced the phosphorylation of YB-1 at S102, which diminishes the interaction between YB-1 and OTUB1."
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"Moreover, SL-0101 restored the interaction between YB-1 and OTUB1 (Fig. 3F) and consequently ameliorated the ubiquitination modification of YB-1 (Fig. 3G)."
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"Co-IP results showed the homeostatic interaction of YB-1 and OTUB1 in cardiomyocytes, which are sensitive to diabetic microenvironment."
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"In accordance with our in vitro findings, U0126 could suppress the ERK phosphorylation, RSK phosphorylation, and subsequent YB-1 S102 phosphorylation, resulting in enhanced interaction between YB-1 and OTUB1 and preserved YB-1 protein expression in diabetic hearts."
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"To explore the interaction between YB-1 and OTUB1, H9c2 cells were coinfected with GFP-tagged YB-1 and FLAG-tagged OTUB1 overexpressing lentivirus for 48 h and also received different interventions described previously."
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"In diabetic mice, aPC ameliorated YB-1 degradation via reducing its K48 ubiquitination through deubiquitinating enzyme otubain-1 (OTUB1) and improving the interaction between YB-1 and OTUB1."
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"Study in vitro and in vivo indicated that hyperglycaemia caused the phosphorylation of S102 site of YB-1 in cardiomyocytes, which weakened the interaction between YB-1 and OTUB1, thus promoting the degradation of YB-1 through ubiquitin-proteasome pathway, leading to aggravation of diabetes cardiomyopathy (Ref."
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"In addition to HACE1, YB-1 also interacts with the deubiquitinase otubain-1 (OTUB1) [ xref ]."
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"Coimmunoprecipitation experiments showed that YB-1 interacts with the deubiquitinase otubain-1, but hyperglycemia-induced phosphorylation of YB-1 at S102 diminished this homeostatic interaction, resulting in ubiquitination and degradation of YB-1."
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"We demonstrate that ERK inhibition with U0126 also suppressed the phosphorylation of the downstream RSK and YB-1 (S102), which stabilized the interaction between YB-1 and otubain-1 and thereby preserved YB-1 protein expression in diabetic hearts."
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