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"We also found that USP28 interacted with STAT3, and stabilized STAT3 by decreasing its polyubiquitination, which indicated that STAT3 was a potential substrate of USP28 (XREF_FIG and XREF_FIG)."

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"This interaction between STAT3 and USP28 was further confirmed by IP with anti-USP28 antibody and then blotting with anti-STAT3 antibody, wherein STAT3 protein was also found in the USP28 immunoprecip[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"The fact that USP28 interacted with STAT3, and both proteins were upregulated in ADPKD kidneys prompted us to speculate that USP28 may regulate STAT3 as a deubiquitinase."

"The deubiquitinating enzyme USP28 mediates STAT3 signaling in non-small-cell lung cancer cells, and USP28 interacts with STAT3 and enhances its stability by inducing the deubiquitination of STAT3 [ xref ]."

"Ubiquitin‐specific peptidase 28 (USP28) is a deubiquitinase, which has been found upregulated in several tumors, and displays its function as an oncoprotein. xref In breast cancer and colon cancer, USP28 was found highly expressed. xref As a deubiquitinase, USP28 bound to c‐Myc protein through an interaction with E3 ligase FBW7α, and USP28 stabilized c‐Myc by decreasing its polyubiquitination, which was essential for cell proliferation in tumors. xref It has also been reported that USP28 knockdown enhanced the radiosensitivity of esophageal cancer cells by destabilizing c‐Myc protein and enhancing the accumulation of HIF‐1α. xref In non‐small cell lung cancer (NSCLC), USP28 was upregulated and predicted a poor index of NSCLC patients. xref In mechanism, USP28 bound to STAT3, and stabilized STAT3 by decreasing its polyubiquitination. xref Thus, inhibiting USP28 could be as a promising strategy for tumor diagnosis or treatment."

"A previous study demonstrated that the deubiquitinating enzyme USP28 directly interacts with STAT3 and increases its stability. xref Thus, regulation of STAT3 acetylation and recruitment of E3 ligase or deubiquitinating enzymes might be associated with the regulation of STAT3 protein stability by SA14."

"Immunoprecipitation was performed to assess whether USP28 interacted with STAT3 or deubiquitinated STAT3."

"USP28 interacted with STAT3, and increased the stability of STAT3 by inducing its deubiquitination."

"USP28 interacted with STAT3 and decreased the polyubiquitination of STAT3, thereby increasing the stability of STAT3."

"USP28 interacted with STAT3 and decreased the polyubiquitination of STAT3, thereby increasing the stability of STAT3."

"USP28 interacts with STAT3 and decreases its polyubiquitination level."

"To evaluate whether USP28 interacted with STAT3, the reciprocal Co-IP was performed."

"As shown in xref , the Co-IP revealed that exogenous USP28 interacted with exogenous STAT3 protein."

"Additionally, the Co-IP in xref showed that endogenous STAT3 also interacted with endogenous USP28."

"We also found that USP28 interacted with STAT3, and stabilized STAT3 by decreasing its polyubiquitination, which indicated that STAT3 was a potential substrate of USP28 ( xref and xref )."

"Immunoprecipitation was performed to assess whether USP28 interacted with STAT3 or deubiquitinated STAT3."

"USP28 interacted with STAT3, and increased the stability of STAT3 by inducing its deubiquitination."

No evidence text available

No evidence text available

"USP28 interacts with STAT3 and decreases its polyubiquitination level."

"To evaluate whether USP28 interacted with STAT3, the reciprocal Co-IP was performed."

"Additionally, the Co-IP in XREF_FIG showed that endogenous STAT3 also interacted with endogenous USP28."