The serine/threonine protein kinase RIO1 is an enzyme encoded by the RIOK1 gene in humans. RIOK1 is an atypical protein found in most archaea and eukaryotes. It belongs to the serine/threonine-specific protein kinase family and has been studied intensively to understand their role in promoting small ribosomal subunits (SSUs). It is suggested that the overexpression or mutation of RIOK 1 gene may lead to dysregulation of its network (in posterior animals-large signal networks at the protein and gene level, which stimulate growth or division by stimulating or limiting nutrient utilization). This has been observed in primary cancer cells and may contribute to the occurrence and development of cancer.
Functions
Although the function of RIOK1 is still unclear, the lack of this protein has been found to confer resistance to a certain type of bacteria called Aeromonas, suggesting its immunosuppressive effect. The feedback loop is a model where RIOK1 can suppress our immune system against bacteria in p38 MAPK and SKN-1. The presence of microorganisms activates the p38 MAPK pathway, which increases the concentration of SKN-1, and will eventually produce the necessary amount of RIOK1 to terminate the pathway.
In addition, RIOK1 also has a potential role in the metabolism of the 40S ribosomal subunit. To be precise, we know that it is related to the maturation of the 40S ribosomal subunit and is necessary for the recovery of PNO1 and NOB1. Both PNO1 and NOB1 are RNA binding protein 40S precursor.
In addition, the RIOK1 protein binding function stands out among other proteins involved in the same activity. For example, in PRMT5 binding involving RIOK1 and PICln, it is suggested that RIOK1 is a more versatile adapter than PICln. RIOK1 also interacts with NCL through its C-terminus, which targets NCL to PRMT5 methylation.
Characterists
RIOK 1 has a molecular weight of 65,583 Da, a basic isoelectric point of 5.84 (predicted pI of various phosphorylated states; pI of unphosphorylated state = 5.84), and a human orthodox 6p24.3 chromosome position.
PTM effect
Effects on modified proteins-protein degradation triggered by K411-m1; protein stabilization triggered by T410-p; ubiquitination, triggered by K411-m1. Effects on biological processes-K411-m1 triggered cell growth was inhibited.
Mutagenesis
Effects of experimental mutations in one or more amino acids on biological properties of proteins. When an amino acid residue changes, we report the change, the name of the mutant (if known), and the effect of the mutation on a protein, cell, or intact organism. When mutations are associated with several point mutations, we add the exact combination of mutations (position and amino acid modification). The mutation in RIOK1 (D324A) eliminated autophosphorylation activity, enhanced binding to the 40S preribosomal subunit, and inhibited processing of 18S-E pre-rRNA to mature 18S rRNA.
Conservation
Looking at multiple sequence alignments, three different RIOK 1: human, mouse and rat modified residues can be compared in the red box.
Reference