RIOK1: A Protein Kinase Implicated in Neurodegenerative Disorders and Cancer

Target Name: RIOK1

NCBI ID: G83732

Other Name(s): Serine/threonine-protein kinase RIO1 | RIOK1 variant 1 | RIO1 | RIOK1_HUMAN | Serine/threonine-protein kinase RIO1 (isoform 1) | RIO kinase 1, transcript variant 1 | OTTHUMP00000015999 | RRP10 | RIO kinase 1 | AD034 | MGC12903 | bA288G3.1 | Prematurely truncated due to insertion of intronic sequence | FLJ30006

RIOK1: A Protein Kinase Implicated in Neurodegenerative Disorders and Cancer

RIOK1 (Serine/threonine-protein kinase RIO1) is a protein that is expressed in various tissues throughout the body, including the brain, heart, and kidneys. It is a key regulator of cell signaling pathways and has been implicated in a number of diseases, including neurodegenerative disorders, cancer, and cardiovascular disease.

One of the key functions of RIO1 is its role as a protein kinase, which means it can catalyze the transfer of a phosphate group from a protein substrate to its catalytic active site. This process is a fundamental aspect of cell signaling and is involved in the regulation of a wide range of cellular processes, including cell growth, differentiation, and survival.

RIOK1 has been shown to be involved in a number of important cellular processes, including the regulation of neurotransmitter release, cell signaling pathways, and the control of inflammation. It has also been implicated in the development and progression of a number of diseases, including neurodegenerative disorders, cancer, and cardiovascular disease.

One of the key challenges in studying RIO1 is its complex structure and the fact that it is expressed in a wide range of tissues. This makes it difficult to study its functions in isolation and to determine exactly how it contributes to the regulation of cellular processes. However, research into RIO1 has identified a number of potential drug targets and biomarkers that may be useful in the development of new treatments for a variety of diseases.

One potential drug target for RIO1 is the inhibition of its activity as a protein kinase. This could be achieved through a variety of methods, including the use of small molecules, antibodies, or other therapeutic agents that specifically target RIO1. By inhibiting RIO1's kinase activity, researchers hope to reduce the activity of this protein and its impact on cellular processes, potentially leading to the development of neurodegenerative disorders, cancer, or cardiovascular disease.

Another potential drug target for RIO1 is the targeting of its serine/threonine site. This site is known as the catalytic active site and is the site where RIO1 catalyzes the transfer of a phosphate group from its protein substrate. By targeting this site, researchers hope to disrupt the catalytic activity of RIO1 and reduce its impact on cellular processes.

In addition to its potential drug targets, RIO1 is also a potential biomarker for a number of diseases. Its expression has been shown to be elevated in a variety of neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease, as well as in the brains of cancer patients. This suggests that RIO1 may be a useful biomarker for the diagnosis and treatment of these disorders.

Overall, RIO1 is a complex and important protein that has a wide range of functions in cellular processes. Its potential as a drug target and biomarker make it an attractive target for researchers to study and develop new treatments for a variety of diseases.

Protein Name: RIO Kinase 1

Functions: Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in processing of 18S-E pre-rRNA to the mature 18S rRNA. Required for the recycling of NOB1 and PNO1 from the late 40S precursor (PubMed:22072790). The association with the very late 40S subunit intermediate may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit (By similarity). Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity). The catalytic activity regulates its dynamic association with the 40S subunit (By similarity). In addition to its role in ribosomal biogenesis acts as an adapter protein by recruiting NCL/nucleolin the to PRMT5 complex for its symmetrical methylation (PubMed:21081503)

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