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Updated: Aug 25, 2026

Visualizing and Quantifying Endonuclease-Based Site-Specific DNA Damage
Published on: August 21, 2021
Degadration of mismatch repair hMutSalpha heterodimer by the ubiquitin-proteasome pathway
Hélène Hernandez-Pigeon1, Guy Laurent, Odile Humbert
1INSERM U563, Centre de Physiopathologie Toulouse Purpan, Institut Claudius Regaud, 20 rue du Pont Saint-Pierre, 31052 Toulouse, France.
Abstract:
Mismatch repair plays a critical role in genome stability. This process requires several proteins including hMSH2/hMSH6 (hMutSalpha) heterodimer involved in the first stage of the process, the mispair recognition. We previously reported that in U937 and HL-60 cell lines, hMSH2 and hMSH6 protein expression was much lower than that in HeLa and KG1a cells. Here, we showed that the decreased expression of hMutSalpha results from differences in the degradation rate of both proteins by the ubiquitin-proteasome pathway. Our data suggest that in human cell lines, ubiquitin-proteasome could play an important role in the regulation of hMutSalpha protein expression, thereby regulating mismatch repair activity.
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