Heat Shock Protein HSP90AB1: Potential Drug Target and Biomarker

Target Name: HSP90AB1

NCBI ID: G3326

HSP90AB1

Heat Shock Protein HSP90AB1: Potential Drug Target and Biomarker

Heat shock 90kDa protein 1 (HSP90AB1) is a protein that is expressed in various cell types and is involved in the heat shock response. It is a key regulator of protein folding and localization, and is implicated in a wide range of cellular processes, including cell survival, growth, and stress resistance.

HSP90AB1 is a member of the heat shock protein (HSP) family, which includes a diverse group of proteins that are involved in the regulation of protein folding and stability. These proteins are characterized by the presence of a unique domains that are involved in their stability and functions, including a heme core, a calamate domain, and a N-terminal domain.

HSP90AB1 is a 16kDa protein that is expressed in various cell types, including muscle, heart, liver, and brain. It is highly conserved, with a calculated pI of 11.0 and a predicted localization in the cytoplasm. HSP90AB1 is involved in a wide range of cellular processes, including cell survival, growth, and stress resistance.

One of the functions of HSP90AB1 is to regulate protein folding and localization. During times of stress, such as increased temperature or the presence of toxins, HSP90AB1 can interact with other proteins to help them fold correctly and be properly localized in the cytoplasm. This is important for ensuring that these proteins function correctly and are not damaged by the stressor.

Another function of HSP90AB1 is to regulate protein stability. HSP90AB1 is involved in the regulation of protein stability by helping to recruit other proteins to the HSP90AB1-folded protein. This can help to ensure that these proteins are properly maintained and are not degraded by the cell.

HSP90AB1 is also involved in the regulation of cellular processes such as cell growth, apoptosis, and inflammation. For example, HSP90AB1 has been shown to be involved in the regulation of cell apoptosis, a process that is important for removing damaged or dysfunctional cells from the body.

In addition to its role in regulating protein folding and stability, HSP90AB1 is also involved in the regulation of cellular signaling pathways. For example, HSP90AB1 has been shown to be involved in the regulation of the unfolded protein response (FPR), a process that is important for the regulation of protein stability and function.

HSP90AB1 is also a potential drug target and biomarker. For example, HSP90AB1 has been shown to be involved in the regulation of cancer cell growth and has been identified as a potential therapeutic target for cancer treatment. In addition, HSP90AB1 has also been shown to be involved in the regulation of inflammation and has potential as a therapeutic target for the treatment of inflammatory diseases.

Overall, HSP90AB1 is a protein that is involved in a wide range of cellular processes and is a potential drug target and biomarker. Further research is needed to fully understand the functions of HSP90AB1 and its potential as a therapeutic target.

Protein Name: Heat Shock Protein 90 Alpha Family Class B Member 1

Functions: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)

The "HSP90AB1 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 HSP90AB1 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;
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•   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

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