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USP49 deubiquitinates FKBP4. 6 / 6
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"Recent studies show that DUBs play essential roles in proliferation, motility, and chemoresistance of malignant cells through stabilizing critical proteins.5 For example, USP49 deubiquitinates FKBP51, which serves as a scaffold for dephosphorylating Ser473 residue at Akt, and further sensitizes pancreatic cancer cells to gemcitabine."
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"USP49 deubiquitinates and stabilizes FKBP51, which in turn induces dephosphorylation of AKT mediated by PHLPP recruitment [165] ."
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"USP49 is a positive regulator of phosphorylation of AKT by deubiquitinating and stabilising FKBP51 which in turn enhances PHLPP ( Luo et al., 2017 )."
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"Mechanistically, USP49 deubiquitinates and stabilizes FKBP51, which in turn enhances PHLPP 's capability to dephosphorylate AKT Furthermore, USP49 inhibited pancreatic cancer cell proliferation and enhanced cellular response to gemcitabine in a FKBP51-AKT-dependent manner."
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"USP49 was shown to inhibit pancreatic cancer cell proliferation and enhance cellular response to gemcitabine by deubiquitinating and stabilizing FKBP51, which in turn enhances PHLPP's capability to de[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Mechanistically, <span class="match term0">USP49</span> deubiquitinates and stabilizes <span class="match term1">FKBP51</span>, which in turn enhances PHLPP's capability to dephosphorylate AKT Furthermore, <span class="match term0">USP49</span> inhibited pancreatic cancer cell proliferation and enhanced cellular response to gemcitabine in a <span class="match term1">FKBP51</span>-AKT-dependent manner."
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