Abstract
The human C-terminal domain small phosphatase 1 (CTDSP1/SCP1) is a protein phosphatase with a conserved catalytic site of DXDXT/V. CTDSP1’s major activity has been identified as dephosphorylation of the 5th Ser residue of the tandem heptad repeat of the RNA polymerase II C-terminal domain (RNAP II CTD). It is also implicated in various pivotal biological activities, such as acting as a driving factor in repressor element 1 (RE-1)-silencing transcription factor (REST) complex, which silences the neuronal genes in non-neuronal cells, G1/S phase transition, and osteoblast differentiation. Recent findings have denoted that negative regulation of CTDSP1 results in suppression of cancer invasion in neuroglioma cells. Several researchers have focused on the development of regulating materials of CTDSP1, due to the significant roles it has in various biological activities. In this review, we focused on this emerging target and explored the biological significance, challenges, and opportunities in targeting CTDSP1 from a drug designing perspective.
Highlights
RNA polymerase II (RNAP II) is the crucial component of a transcription apparatus, and orchestrates the post-transcriptional regulation and modification of mRNA
A new study has suggested that cell division associated 3 protein (CDCA3) could be an enzymatic substrate for CTDSP1 [15]
Apart from these known functionalities, a recent study related to cancer invasion exhibited the exciting results that CTDSP1 dephosphorylates Twist-related protein (TWIST) and regulates cancer cell migration [16]
Summary
RNA polymerase II (RNAP II) is the crucial component of a transcription apparatus, and orchestrates the post-transcriptional regulation and modification of mRNA. A new study has suggested that cell division associated 3 protein (CDCA3) could be an enzymatic substrate for CTDSP1 [15]. Apart from these known functionalities, a recent study related to cancer invasion exhibited the exciting results that CTDSP1 dephosphorylates Twist-related protein (TWIST) and regulates cancer cell migration [16]. Given all these characteristics, we are seeking to prove that CTDSP1 can be considered as a potential drug target. We will focus on contemporary techniques of molecular docking, which will help make progress towards successful targeting of CTDSP1
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