PRC1: A Protein Regulator of Cytokinesis in Cancer and Inflammatory Diseases

Target Name: PRC1

NCBI ID: G9055

PRC1

PRC1: A Protein Regulator of Cytokinesis in Cancer and Inflammatory Diseases

Cytokinesis is a critical process involved in cell division and growth, which is highly regulated by a complex network of proteins. One of the key proteins involved in regulating cytokinesis is PRC1 (Protein regulator of cytokinesis 1), a transmembrane protein that belongs to the FERMT3 (F-actinin-like) family. In this article, we will discuss the role of PRC1 in cell cytokinesis, its potential as a drug target, and its involvement in cancer and inflammatory diseases.

Structure and Function

PRC1 is a 21-kDa protein that was identified as a gene mutated in many breast and ovarian cancers. It is highly conserved across various species, including human, and has been shown to be involved in the regulation of cytokinesis in various cell types. PRC1 functions as a negative regulator of the actinin-based cytokinesis process, which is characterized by the recruitment of actinin, a protein that can interact with actinin-like molecules on the plasma membrane, to the cortical actin network.

Actinin-based cytokinesis is a highly regulated process that involves the recruitment of actinin to the actin network, which then pulls the chromosomes towards the center of the cell. This process is critical for cell growth, apoptosis, and cytokinesis. PRC1 is involved in regulating actinin-based cytokinesis by recruiting actinin to the network and preventing its accumulation at the outer cortex.

In addition to its role in regulating actinin-based cytokinesis, PRC1 is also involved in the regulation of cell adhesion and migration. It has been shown to be involved in the regulation of tight junction formation in various cell types and has been implicated in the regulation of cell migration.

Drug Target Potential

PRC1 is a potential drug target for various diseases, including cancer and inflammatory diseases. Its involvement in actinin-based cytokinesis and its ability to regulate cell adhesion and migration make it an attractive target for cancer treatments.

PRC1 has been shown to be overexpressed in various types of cancer, including breast, ovarian, and prostate cancers. It has also been shown to be involved in the regulation of cell adhesion and migration in various types of cancer. This suggests that targeting PRC1 may be an effective way to treat cancer by inhibiting its role in actinin-based cytokinesis and cell adhesion.

In addition to its potential as a cancer drug, PRC1 may also be a useful biomarker for monitoring the effectiveness of cancer treatments. Its involvement in actinin-based cytokinesis and cell adhesion make it an attractive target for diagnostic tests for various types of cancer.

Pathway Analysis

The regulation of actinin-based cytokinesis by PRC1 is complex and involves multiple interactions with other proteins. It involves a direct interaction with actinin, which is known as the N-terminus of PRC1. This interaction is critical for the recruitment of actinin to the network.

In addition to its direct interaction with actinin, PRC1 also interacts with several other proteins, including the cytoskeleton, the endoplasmic reticulum, and various signaling pathways. These interactions play a critical role in regulating actinin-based cytokinesis and the overall cytoskeleton structure.

Conclusion

PRC1 is a protein that plays a critical role in regulating actinin-based cytokinesis in various cell types. Its involvement in the regulation of cell adhesion and migration makes it an attractive target for cancer treatments. PRC1 may also be a useful biomarker for monitoring the effectiveness of cancer treatments.

Targeting PRC1

Protein Name: Protein Regulator Of Cytokinesis 1

Functions: Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436)

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