HPF1: A Potential Drug Target for TGF-β and Wnt Signaling Pathways

Target Name: HPF1

NCBI ID: G54969

HPF1

Other Name(s): UPF0609 protein C4orf27 | Histone PARylation factor 1 | histone PARylation factor 1 | C4orf27 | HPF1_HUMAN

HPF1: A Potential Drug Target for TGF-β and Wnt Signaling Pathways

HPF1 (UPF0609 protein C4orf27), also known asHPF1-C4orf27, is a protein that is expressed in various tissues and cell types in the human body. It is a member of the superfamily of transmembrane protein (SMP), which includes a variety of structurally similar proteins that are involved in various cellular processes. One of the key functions of HPF1 is its role in the regulation of cell signaling pathways, particularly those that are involved in cell growth, differentiation, and survival.

In recent years, researchers have become increasingly interested in the potential of HPF1 as a drug target or biomarker. This is because the protein is known to play a role in the regulation of several key signaling pathways, including the TGF-β pathway. TGF-β is a well-known signaling pathway that is involved in the regulation of cell growth, differentiation, and survival, and it is thought to be involved in the development and progression of many diseases, including cancer.

One of the key reasons for the interest in HPF1 as a drug target is its role in the regulation of TGF-β signaling. TGF-β signaling is involved in the regulation of cell growth, and it is thought to play a key role in the development and progression of many diseases, including cancer. Researchers have identified several TGF-β signaling pathways that are involved in the regulation of cell growth and differentiation, and they are now looking for potential drug targets.

HPF1 is one of the proteins that has been identified as a potential drug target in the TGF-β pathway. Studies have shown that HPF1 plays a role in the regulation of TGF-β signaling by interacting with several key components of the pathway, including the protein Smad4. Smad4 is a key component of the TGF-β pathway, and it is thought to play a key role in the regulation of TGF-β signaling.

In addition to its role in TGF-β signaling, HPF1 is also involved in the regulation of several other signaling pathways that are important for cell growth and differentiation. For example, it is known to play a role in the regulation of the Wnt signaling pathway, which is involved in the regulation of cell growth and the development of tissues. It is also thought to play a role in the regulation of theNotch signaling pathway, which is involved in the regulation of cell survival and the development of tissues.

As a result of its involvement in several key signaling pathways, HPF1 is thought to be a promising drug target for a variety of diseases. For example, it is being studied as a potential therapeutic agent for the treatment of cancer, as well as a variety of other diseases, including cardiovascular disease, neurodegenerative diseases, and autoimmune diseases.

In conclusion, HPF1 is a protein that is expressed in various tissues and cell types in the human body and is involved in the regulation of several key signaling pathways, including TGF-β and Wnt signaling pathways. As a result, it is thought to be a promising drug target for a variety of diseases. Further research is needed to fully understand the role of HPF1 as a drug target and to develop effective therapies for the treatment of these diseases.

Protein Name: Histone PARylation Factor 1

Functions: Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response (PubMed:28190768, PubMed:29480802, PubMed:29954836, PubMed:33186521, PubMed:32028527, PubMed:32939087, PubMed:34486521, PubMed:34874266, PubMed:34210965, PubMed:34625544, PubMed:33589610, PubMed:34732825, PubMed:33683197, PubMed:34795260, PubMed:34108479). Initiates the repair of double-strand DNA breaks: recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins (PubMed:28190768, PubMed:29480802, PubMed:29954836, PubMed:32028527, PubMed:32939087, PubMed:34486521, PubMed:34874266, PubMed:34625544, PubMed:33589610, PubMed:34732825, PubMed:33683197, PubMed:34795260). Serine ADP-ribosylation of target proteins, such as histones, promotes decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:27067600, PubMed:28190768, PubMed:32939087, PubMed:33589610). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802). HPF1 acts by completing the active site of PARP1 and PARP2: forms a composite active site composed of residues from HPF1 and PARP1 or PARP2 (PubMed:32028527, PubMed:33589610). While HPF1 promotes the initiation of serine ADP-ribosylation, it restricts the polymerase activity of PARP1 and PARP2 in order to limit the length of poly-ADP-ribose chains (PubMed:34732825, PubMed:33683197, PubMed:34795260). HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1 (PubMed:29954836, PubMed:30257210)

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