Customize Consent Preferences

We use cookies to help you navigate efficiently and perform certain functions. You will find detailed information about all cookies under each consent category below.

The cookies that are categorized as "Necessary" are stored on your browser as they are essential for enabling the basic functionalities of the site. ... 

Always Active

Necessary cookies are required to enable the basic features of this site, such as providing secure log-in or adjusting your consent preferences. These cookies do not store any personally identifiable data.

No cookies to display.

Functional cookies help perform certain functionalities like sharing the content of the website on social media platforms, collecting feedback, and other third-party features.

No cookies to display.

Analytical cookies are used to understand how visitors interact with the website. These cookies help provide information on metrics such as the number of visitors, bounce rate, traffic source, etc.

No cookies to display.

Performance cookies are used to understand and analyze the key performance indexes of the website which helps in delivering a better user experience for the visitors.

No cookies to display.

Advertisement cookies are used to provide visitors with customized advertisements based on the pages you visited previously and to analyze the effectiveness of the ad campaigns.

No cookies to display.

Skip to main content

Foundation Young Investigator Gets a New Angle on NF2

By December 14, 2009December 4th, 2023Awareness, NF2-SWN

NF2 researchers have puzzled over how the NF2 gene protein product merlin actually works in the cell. Why does this matter? Because understanding this will help us better figure out how to make drugs that correct merlin function in NF2 tumors and stop them from growing. In a new paper* (abstract) published in Molecular Cell Biology, Children’s Tumor Foundation Young Investigator Awardee Timmy Mani (University of Cincinnati) with a team led by his mentor Dr. Wallace Ip provide a new and unique view of merlin that might advance this area. It has long been known that merlin is related to proteins from the Ezrin Radixin-Moesin (ERM) protein family. ERM proteins are regulated by switching from a ‘closed’ to an ‘open’ conformation, and it has been thought merlin is the same. Mani and colleagues developed a series of probes that allowed them to ‘visualize’ merlin by fluorescence resonance energy transfer (FRET), as purified protein and in living cells. They found something new and unexpected: merlin exists in a stable, closed conformation but when activated undergoes a more subtle change than previously thought. These studies add to a recently growing body of evidence that challenge the standard thinking in the NF2 field. Also, though early stage, this type of research can inform the development of drug therapies aimed at targeting and restoring merlin function, and providing tumor treatments. This work was supported by the NIH, DOD CDMRP and the Children’s Tumor Foundation.

Close Menu