Author response: Minimized human telomerase maintains telomeres and resolves endogenous roles of H/ACA proteins, TCAB1, and Cajal bodies
Year: 2016
Type: peer-review
Abstract: Most cells in the human body can only divide a certain number of times before they die. This is because regions called telomeres at the ends of the cell’s DNA get shorter every time the cell divides, to the point that they disappear and halt cell growth. Particular types of cells – including some stem cells and cancer cells – can avoid death and continue to divide indefinitely because they produce an enzyme called telomerase that extends the telomere regions. The process by which the telomerase enzyme binds to and lengthens the DNA has several stages and involves many different proteins. One of the stages involves moving telomerase from the sites where it is assembled within the cell to a place where it can find telomeres in need of elongation (different areas within the cell compartment called the nucleus). Structures inside the nucleus called Cajal bodies were thought to help the enzyme bind to the telomeres. It is not clear why the process of extending telomeres is so complex. Vogan et al. engineered altered versions of telomerase that use simpler pathways to bind to and act on telomeres and inserted them into ‘pluripotent’ stem cells and cancer cells from humans. The experiments show that a pathway that helps to move the enzyme from its normal storage place in the nucleus is less important for extending telomeres in cancer cells than in pluripotent stem cells. Unexpectedly, Cajal bodies are not critical for bringing telomerase into contact with the telomeres in either cell type. The findings show that many of the proteins involved in extending telomeres in cells are not strictly essential. The simplified pathway developed by Vogan et al. opens up new opportunities to study the details of how telomerase extends telomeres.
Institution: University of California, Berkeley
Language: English
Subfield: Physiology
Field: Medicine
Domain: Health Sciences
Open Access status: gold
OpenAlex ID: W2986503198