IndraLab

Statements

USP29 is phosphorylated. 12 / 12
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"Phosphorylation could regulate protein‐protein interactions or the enzymatic activity of deubiquitinases. [ xref ] We next investigated whether the effect of CDK1 on TWIST1 and malignant processes in TNBC is mediated by the phosphorylation of USP29."
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"These results indicate that CDK1‐mediated phosphorylation of USP29 is indispensable for its enzymatic activity toward TWIST1 as well as the TWIST1‐dependent malignant phenotypes in TNBC."
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"Furthermore, CDK1‐mediated phosphorylation of USP29 governs TWIST1 stability and oncogenic functions."
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"Mechanistically, CDK1‐mediated phosphorylation of USP29 is essential for its deubiquitinase activity toward TWIST1 and TWIST1 driven‐malignant phenotypes in TNBC, which could be markedly mitigated by the genetic ablation or pharmacological inhibition of CDK1."
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"CDK1, a USP29 activator, facilitates this process through USP29 phosphorylation, enhancing the TWIST1-driven malignant phenotype [ xref ]."
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"CDK1 Binds and Phosphorylates USP29."
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"First, we identify that CDK1 binds and phosphorylates USP29 at Ser575, Thr578, and Ser672, while the phosphorylation deficient 3A mutation almost abolishes the phosphorylation of USP29 (Figure  xref and Figure xref , Supporting Information)."
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"These results dictate that CDK1‐mediated phosphorylation of USP29 is crucial for its deubiquitinase activity toward TWIST1."
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"We next examined the function of CDK1‐mediated phosphorylation of USP29 on TWIST1‐drivened malignant processes."
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"As shown in Figure  xref , Figure xref (Supporting Information), the phosphorylation of USP29 was detected in both MDA‐MB‐231 and BT549 cells by using phospho‐CDK substrate antibody and the genetic ablation or the pharmacological inhibition of CDK1 by RO‐3306 could significantly reduce this phosphorylation event (Figure  xref , Figure xref , Supporting Information)."
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"As shown in Figure  xref and Figure xref (Supporting Information), the single mutation of USP29 S575A, T578A, or S672A only mildly decreased the phosphorylation of USP29, while the phosphorylation‐deficient 3A mutation (S575A/T578A/S672) almost completely abolished it."
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"We next examined whether CDK1‐mediated phosphorylation of USP29 could affect the ubiquitination level of TWIST1."
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