IndraLab

Statements

USP36 binds PRIMPOL. 11 / 11
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"USP36 interacts with PrimPol via its USP domain."
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"Next, we studied how HU treatment promoted the interaction between USP36 and PrimPol."
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"On the other hand, in cancer cells, higher expression of USP36 might render cancer cells resistant to replication stress, while lower USP36 level or inhibition of USP36-PrimPol axis might sensitize cancer cells to genotoxic insults."
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"Overall, these results suggest that USP36 interacts with PrimPol at stressed replication forks in cells."
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"Cancer cells generally have higher replication stress, and the USP36-PrimPol axis might be required to adapt to this stress."
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"Few dots that represent the interaction of USP36 and PrimPol were observed in the nuclei in unstressed cells."
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"Moreover, treatment with the replication-damaging agent hydroxyurea (HU) promoted the interaction between USP36 and PrimPol (Figure xref , D)."
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"In light of the above findings, we tested whether USP36 might physically interact with PrimPol in cells."
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"Next, we tested whether these two lysine residues (K329R and K338R) were essential for the regulation of USP36-PrimPol interaction."
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"We further confirmed the close interaction between USP36 and PrimPol by proximity ligation assay (PLA)."
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"In ovarian cancer tissues, USP36 overexpression is observed to positively correlate with the level of PrimPol expression and poor prognosis, indicating that the USP36-PrimPol axis may play an important regulatory mechanism in the cancer pathogenesis and treatment."
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