Target Name: PSMC3IP
NCBI ID: G29893
Review Report on PSMC3IP Target / Biomarker Content of Review Report on PSMC3IP Target / Biomarker
PSMC3IP
Other Name(s): PSMC3 interacting protein, transcript variant 1 | nuclear receptor coactivator GT198 | TBP-1 interacting protein | Homologous-pairing protein 2 homolog (isoform 2) | tat-binding protein 1-interacting protein | GT198 alternative | TBPIP | Proteasome 26S ATPase subunit 3-interacting protein | PSMC3 interacting protein | HOP2_HUMAN | PSMC3-interacting protein | Nuclear receptor coactivator GT198 | TBP-1-interacting protein | HUMGT198A | Homologous-pairing protein 2 homolog (isoform 1) | DBD-interacting | ODG3 | GT198 | HOP2 | PSMC3 interacting protein, transcript variant 2 | proteasome 26S ATPase subunit 3-interacting protein | Tat-binding protein 1-interacting protein | PSMC3IP variant 1 | Homologous-pairing protein 2 homolog | PSMC3IP variant 2

PSMC3IP: A Potential Drug Target and Biomarker for the Treatment of Prostate Cancer

Introduction

Prostate cancer is a leading cause of cancer-related deaths worldwide, with an estimated 1,000 new cases and 28,000 deaths in the United States in 2020. The five-year survival rate for prostate cancer is 95%, but the incidence of the disease increases with age, and survival rates decrease due to the high recurrence rates. Therefore, identifying and targeting potential drug targets is crucial for the development of more effective therapies.

PSMC3IP, a protein called PSMC3IP (protein server CPU interacting protein, transcript variant 1), has been identified as a potential drug target for the treatment of prostate cancer. In this article, we will discuss PSMC3IP, its function, potential drug targets, and its potential as a biomarker.

PSMC3IP: A Protein Structure and Function

PSMC3IP is a 25 kDa protein that is expressed in a variety of tissues, including skeletal muscles, heart, brain, and prostate. It is a member of the PSMC family, which includes PSMC1, PSMC2, PSMC3, PSMC4, and PSMC5. These proteins are involved in the regulation of muscle contractions and have been implicated in the development and progression of various diseases, including cancer.

PSMC3IP has a unique structure that consists of a catalytic domain, a transmembrane region, and an N-terminus. The catalytic domain is composed of a single alpha-helix and a gamma-sheet, which contain the protein's active site and the regions responsible for catalyzing chemical reactions. The transmembrane region is composed of a single sheet that spans the entire cell membrane and is involved in the regulation of protein access to the cell surface. The N-terminus is a long terminal region that contains a variety of coiled-coil structures that are involved in protein-protein interactions and may be involved in the regulation of protein stability.

PSMC3IP's Function

PSMC3IP is involved in the regulation of a variety of cellular processes, including cell signaling, protein synthesis, and microtubule dynamics. It is a key regulator of the myosin ATPase complex, which is responsible for generating force during muscle contractions. In cancer cells, the myosin ATPase complex is often overexpressed, leading to muscle rigidity and the development of a more resistant to treatment of muscle cancer.

PSMC3IP has also been shown to be involved in the regulation of protein synthesis and stability. It has been shown to interact with the protein tyrosine kinase (TK) and the nuclear factor of activating transcription factor 3 (NFAT), which are involved in the regulation of protein synthesis and stability, respectively. Overexpression of PSMC3IP has been shown to increase the levels of these transcription factors, leading to an increase in protein synthesis and stability.

PSMC3IP's Potential as a Drug Target

The potential of PSMC3IP as a drug target is due to its involvement in the regulation of cellular processes that are often disrupted in cancer cells. By targeting PSMC3IP, researchers hope to develop new therapies that can inhibit its activity and disrupt its role in the development and progression of cancer.

One potential approach to targeting PSMC3IP is to use small molecules that can inhibit its activity. For example, a variety of compounds have been shown to inhibit the activity of PSMC3IP, including inhibitors of the myosin ATPase complex, protein tyrosine kinase, and NFAT. These compounds have been shown to be effective in preclinical studies for the treatment of prostate cancer.

PSMC3IP has also been shown to interact with several drugs that are currently used in the treatment of prostate cancer. For example,

Protein Name: PSMC3 Interacting Protein

Functions: Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3. Acts as a tissue specific coactivator of hormone-dependent transcription mediated by nuclear receptors

The "PSMC3IP Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about PSMC3IP comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets

PSMC4 | PSMC5 | PSMC6 | PSMD1 | PSMD10 | PSMD10P1 | PSMD11 | PSMD12 | PSMD13 | PSMD14 | PSMD2 | PSMD3 | PSMD4 | PSMD4P1 | PSMD5 | PSMD6 | PSMD6-AS2 | PSMD7 | PSMD8 | PSMD9 | PSME1 | PSME2 | PSME2P2 | PSME2P3 | PSME3 | PSME3IP1 | PSME4 | PSMF1 | PSMG1 | PSMG1-PSMG2 heterodimer | PSMG2 | PSMG3 | PSMG3-AS1 | PSMG4 | PSORS1C1 | PSORS1C2 | PSORS1C3 | PSPC1 | PSPH | PSPHP1 | PSPN | PSRC1 | PSTK | PSTPIP1 | PSTPIP2 | PTAFR | PTAR1 | PTBP1 | PTBP2 | PTBP3 | PTCD1 | PTCD2 | PTCD3 | PTCH1 | PTCH2 | PTCHD1 | PTCHD1-AS | PTCHD3 | PTCHD3P1 | PTCHD3P2 | PTCHD4 | PTCRA | PTCSC2 | PTCSC3 | PTDSS1 | PTDSS2 | PTEN | PTENP1 | PTENP1-AS | PTER | PTF1A | PTGDR | PTGDR2 | PTGDS | PTGER1 | PTGER2 | PTGER3 | PTGER4 | PTGER4P2-CDK2AP2P2 | PTGES | PTGES2 | PTGES2-AS1 | PTGES3 | PTGES3L | PTGES3L-AARSD1 | PTGES3P1 | PTGES3P2 | PTGES3P3 | PTGFR | PTGFRN | PTGIR | PTGIS | PTGR1 | PTGR2 | PTGR3 | PTGS1 | PTGS2 | PTH | PTH1R | PTH2