Unlocking the Potential of DNAJC9 (SB73): A Promising Drug Target and Biomarker

Target Name: DNAJC9

NCBI ID: G23234

Unlocking the Potential of DNAJC9 (SB73): A Promising Drug Target and Biomarker

DNAJC9 (SB73) is a gene that encodes a protein known as DNAJC9, which is a key regulator of microtubules, a vital structure that organizes and transports chromosomes within the nucleus of a cell. The identification of DNAJC9 as a potential drug target and biomarker has significant implications for the development of new treatments for various diseases, including cancer, neurodegenerative disorders, and developmental disorders.

The Protein encoded by DNAJC9

DNAJC9 is a 21-kDa protein that plays a crucial role in the regulation of microtubule dynamics and stability. It is composed of multiple domains, including an N-terminal transmembrane domain, a coiled-coil domain, and a C-terminal T-loop domain. The N-terminal transmembrane domain is responsible for the protein's ability to interact with the microtubules, while the coiled-coil domain and T-loop domain contribute to the protein's stability and structural integrity.

DNAJC9 functions as a negative regulator of microtubule dynamics, which means that it prevents the formation of new microtubules when existing ones are already in place. This regulation is critical for maintaining the proper organization and function of cells, as misregulation of microtubules can lead to various diseases, including cancer, neurodegenerative disorders, and developmental disorders.

The Potential of DNAJC9 as a Drug Target

The identification of DNAJC9 as a potential drug target has significant implications for the development of new treatments for various diseases. One of the primary targets of DNAJC9 is the regulation of cancer cell growth and progression. DNAJC9 has been shown to play a role in the regulation of cell division, and studies have shown that inhibiting its function can lead to a reduction in cancer cell growth and the formation of new tumors.

DNAJC9 has also been shown to be involved in the regulation of neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. These conditions are characterized by the progressive loss of brain cells, which is thought to be due to the misregulation of microtubules. By targeting DNAJC9, researchers may be able to develop new treatments for neurodegenerative disorders.

In addition to its potential therapeutic applications, DNAJC9 has also been shown to be a promising biomarker for the diagnosis and monitoring of various diseases. The regulation of microtubule dynamics is a critical process that is involved in the development and maintenance of tissues, and alterations in microtubule dynamics can be indicative of underlying cellular changes. By measuring the levels of DNAJC9, researchers may be able to develop new diagnostic tests for various diseases, including cancer, neurodegenerative disorders, and developmental disorders.

The Potential of DNAJC9 as a Biomarker

DNAJC9 has also been shown to be a potential biomarker for various diseases. The regulation of microtubule dynamics is a critical process that is involved in the development and maintenance of tissues, and alterations in microtubule dynamics can be indicative of underlying cellular changes. By measuring the levels of DNAJC9, researchers may be able to develop new diagnostic tests for various diseases, including cancer, neurodegenerative disorders, and developmental disorders.

One of the primary applications of DNAJC9 as a biomarker is its potential to detect cancer at an early stage. Many cancer treatments are designed to kill cancer cells, but it is often difficult to detect the presence of cancer at an early stage. DNAJC9 has

Protein Name: DnaJ Heat Shock Protein Family (Hsp40) Member C9

Functions: Acts as a dual histone chaperone and heat shock co-chaperone (PubMed:33857403). As a histone chaperone, forms a co-chaperone complex with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2 in histone H3-H4 heterodimer recognition and facilitate the assembly of histones into nucleosomes (PubMed:33857403). May also act as a histone co-chaperone together with TONSL (PubMed:33857403). May recruit histone chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers (PubMed:33857403). Also plays a role as co-chaperone of the HSP70 family of molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8 (PubMed:17182002, PubMed:33857403). As a co-chaperone, may play a role in the recruitment of HSP70-type molecular chaperone machinery to histone H3-H4 substrates, thereby maintaining the histone structural integrity (PubMed:33857403). Exhibits activity to assemble histones onto DNA in vitro (PubMed:33857403)

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