60S ribosomal protein L26
60S ribosomal protein L26 is a protein that in humans is encoded by the RPL26 gene. This protein is a component of the 60S subunit of the ribosome, playing a critical role in the protein synthesis process. Ribosomes, consisting of two subunits, 40S and 60S, are essential for the translation of mRNA into protein. The 60S ribosomal protein L26 is involved in the assembly and structural stability of the ribosome, facilitating the correct positioning of the mRNA and tRNAs during translation.
Function[edit | edit source]
The primary function of the 60S ribosomal protein L26 is to contribute to the formation and function of the ribosome. It participates in the early stages of ribosome assembly within the nucleolus and is essential for the proper assembly of other ribosomal proteins and rRNA into a functional 60S subunit. Once the ribosome is assembled, RPL26 plays a role in the translation process, ensuring that proteins are synthesized accurately and efficiently. This protein is also implicated in cellular processes such as cell growth, cell cycle regulation, and response to cellular stress.
Gene[edit | edit source]
The RPL26 gene is located on chromosome 17 in humans. It contains several exons and introns, and its expression is tightly regulated to meet the cellular demand for ribosomes, which varies according to the cell's growth and division cycle. Mutations or alterations in the expression of the RPL26 gene can affect ribosome function and have been linked to various human diseases, including cancer.
Clinical Significance[edit | edit source]
Alterations in the expression or function of 60S ribosomal protein L26 can have significant clinical implications. Given its essential role in protein synthesis, any disruption in the function of RPL26 can lead to defects in ribosome biogenesis or function, contributing to diseases such as Diamond-Blackfan anemia and cancer. In cancer, changes in ribosome biogenesis and function can lead to increased production of proteins that promote tumor growth and survival. Research is ongoing to understand the specific mechanisms by which RPL26 contributes to disease and to explore potential therapeutic targets within the ribosome biogenesis pathway.
See Also[edit | edit source]
 | This protein-related article is a stub. You can help WikiMD by expanding it. |
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
|
WikiMD's Wellness Encyclopedia |
| Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD
