IndraLab

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OTUD3 deubiquitinates KPTN. 4 / 4
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"Results revealed that exogenous KPTN was indeed ubiquitinated, and the presence of OTUD3 reduced the level of KPTN ubiquitination in a manner directly proportional to OTUD3 protein levels."
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"We found that OTUD3 significantly deubiquitinates KPTN, effectively removing polyubiquitin chains on the lysine 49 residue."
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"OTUD3’s knockout leads to abnormal mTORC1 pathway activation, resulting in Warburg effect induction and increased synthesis-related metabolism.While our study elucidates how OTUD3 regulates the mTORC1 pathway by deubiquitinating KPTN and influencing the recruitment of the KICSTOR complex to GATOR1, many aspects remain to be fully explored."
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"3.2 OTUD3 promoted the deubiquitination of KPTN but did not affect its protein levels."
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