SPRTN: A Potential Drug Target for DNA Damage Protein Targeting

Target Name: SPRTN

NCBI ID: G83932

SPRTN: A Potential Drug Target for DNA Damage Protein Targeting

Introduction

Sprouting RNA-protein domains (SRTNs) are a family of proteins that play a crucial role in various cellular processes, including DNA damage repair and gene expression. DNA damage repair is a critical process that helps cells recover from DNA mutations and fissions that can result from exposure to mutagenic agents, such as radiation, chemicals, or viruses. The ability of SRTNs to detect and repair DNA damage is crucial for maintaining cellular health and homeostasis.

SPRTNs are composed of a unique combination of RNA and protein domains that give them unique structural features. They have a characteristic stem-loop structure that is composed of a series of RNA domains that are flanked by protein domains. domains allows them to transcribe and translated into proteins with unique functions.

One of the key functions of SRTNs is their ability to interact with DNA damage repair factors, which are proteins that help to repair damaged DNA. These factors include DNA repair proteins, such as DNA polymerase, which are essential for copying the damaged DNA strand back to its original state, and cell cycle proteins, which help to ensure that damaged DNA is properly segregated into the cell's two chromosomes.

SPRTNs have also been shown to play a key role in regulating gene expression. They can interact with various transcription factors, including RNA polymerase II, to promote the translation of RNA into protein. This function is critical for the development and maintenance of cellular diversity, as it allows cells to respond to various stimuli and ensure that their genetic information is accurately replicated.

In addition to their role in DNA damage repair and gene expression, SRTNs have also been shown to play a key role in the regulation of cellular signaling pathways. They can interact with various signaling proteins, including tyrosine kinases, to regulate the signaling pathways that are responsible for cellular growth, differentiation, and survival.

The Importance of SPRTNs in Cancer

The regulation of DNA damage repair is a critical function of cancer cells, as mutations in DNA can lead to the development of cancer. Cancer cells have the ability to repair DNA damage, but they often have defects in their DNA repair capabilities, which allows them to continue to grow and multiply uncontrollably.

SPRTNs have been shown to play a key role in the regulation of DNA damage repair in cancer cells. They can interact with DNA repair factors to promote the repair of DNA damage, which is critical for the development and maintenance of cancer cells. In addition, SPRTNs have also been shown to play a key role in the regulation of cell cycle progression, which is the process by which cells grow and divide.

SPRTNs have also been shown to contribute to the development of various types of cancer, including breast, ovarian, and prostate cancers. These cancers can arise due to various factors, including genetic mutations, where the DNA is repairable but has a mistake, or due to the loss of gene expression, where the DNA repair capabilities of the cells are defective.

Targeting SPRTNs for Cancer Treatment

The development of cancer can be a difficult and complex process, and the development of effective cancer treatments can be challenging. However, recent studies have shown that SPRTNs may be an effective drug target for cancer treatment.

One potential approach to targeting SPRTNs for cancer treatment is to use small molecules that can inhibit the activity of SPRTNs. These small molecules can be designed to interact with specific SPRTNs, such as SPRTN-1, SPRTN-2, or SPRTN-3, and disrupt their ability

Protein Name: SprT-like N-terminal Domain

Functions: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:27852435, PubMed:27871366, PubMed:27871365, PubMed:32649882, PubMed:30893605). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (PubMed:27852435, PubMed:27871366, PubMed:27871365, PubMed:32649882). Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis (PubMed:27852435, PubMed:27871366, PubMed:27871365, PubMed:32649882). Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (PubMed:27871366). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs (By similarity). SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage (PubMed:22902628, PubMed:23042605, PubMed:23042607, PubMed:32152270). Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation (PubMed:31316063). Does not activate CHEK1 in response to DNA damage (PubMed:31316063). May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA (PubMed:22681887, PubMed:22894931, PubMed:22902628, PubMed:22987070). Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (PubMed:22681887)

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