KIF24: A Potential Drug Target and Biomarker (G347240)

Target Name: KIF24

NCBI ID: G347240

Other Name(s): KIF24_HUMAN | Kinesin family member 24 | Kinesin-like protein KIF24 | MGC125677 | C9orf48 | bA571F15.4 | MGC125678 | FLJ43884 | FLJ10933 | OTTHUMP00000021249 | kinesin family member 24

KIF24: A Potential Drug Target and Biomarker

KIF24 is a protein that is expressed in various tissues of the body, including the brain, heart, lungs, and gastrointestinal tract. It is a member of the Kallikrein-related peptidases (KAPs) family, which includes a variety of enzymes that regulate proteolytic enzymes and other cellular processes.

KIF24 is unique among its kind because of its ability to interact with multiple cell types and tissues. Its expression has been observed in a wide range of biological samples, including plasma, tissue, and organ extracts, making it a promising biomarker for a variety of diseases.

One of the key functions of KIF24 is its role in regulating the activity of proteases, which are enzymes that break down other proteins. In many cases, proteases are important for both normal cellular function and the development of diseases. For example, proteases can be involved in cell signaling, tissue repair, and inflammation. However, when they become abnormally active or out of control, they can contribute to a wide range of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

KIF24 is also involved in regulating the activity of other cellular processes, including cell adhesion, migration, and the formation of tight junctions. These processes are important for maintaining the integrity and function of tissues and organs, and are often disrupted in diseases such as cancer and neurodegenerative diseases.

KIF24 has also been shown to play a role in the regulation of inflammation. Its expression has been observed in a variety of inflammatory diseases, including arthritis, asthma, and multiple sclerosis. Additionally, KIF24 has been shown to have anti-inflammatory effects, which may make it a potential therapeutic target for these diseases.

In addition to its potential therapeutic applications, KIF24 is also a drug target. Its expression has been shown to be regulated by a variety of factors, including cytokines, chemokines, and other signaling molecules. This makes it an attractive target for drugs that are designed to modulate its activity.

One of the challenges in studying KIF24 is its complex expression pattern. Its expression is observed in a wide range of tissues and cells, and it can be difficult to isolate and study it in a controlled environment. Additionally, the functions of KIF24 are still not fully understood, and more research is needed to determine its role in the development and progression of various diseases.

Despite these challenges, the potential of KIF24 as a drug target and biomarker is significant. Its ability to interact with multiple cell types and tissues makes it a promising target for a variety of therapeutic approaches. Additionally, its role in regulating the activity of proteases and other cellular processes suggests that it may have a wide range of potential applications in a variety of diseases.

In conclusion, KIF24 is a protein that is expressed in various tissues of the body that is involved in the regulation of proteolytic enzymes and other cellular processes. Its unique ability to interact with multiple cell types and tissues makes it a promising biomarker and potential therapeutic target for a variety of diseases. Further research is needed to fully understand its functions and potential applications.

Protein Name: Kinesin Family Member 24

Functions: Microtubule-dependent motor protein that acts as a negative regulator of ciliogenesis by mediating recruitment of CCP110 to mother centriole in cycling cells, leading to restrict nucleation of cilia at centrioles. Mediates depolymerization of microtubules of centriolar origin, possibly to suppress aberrant cilia formation (PubMed:21620453). Following activation by NEK2 involved in disassembly of primary cilium during G2/M phase but does not disassemble fully formed ciliary axonemes. As cilium assembly and disassembly is proposed to coexist in a dynamic equilibrium may suppress nascent cilium assembly and, potentially, ciliar re-assembly in cells that have already disassembled their cilia ensuring the completion of cilium removal in the later stages of the cell cycle (PubMed:26290419). Plays an important role in recruiting MPHOSPH9, a negative regulator of cilia formation to the distal end of mother centriole (PubMed:30375385)

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