There are many processes and signals in cells that must be turned on and off, sometimes very quickly. How is this done? One important way is via post-translational modification of proteins such as phosphorylation or dephosphorylation. In her first talk, Dr. Anne Bertolotti introduces us to protein phosphatases, the enzymes that remove phosphate from proteins and work in opposition to protein kinases. She gives a brief history of the early experiments that showed that phosphatases are vital to regulating the stability, localization and interactions of many proteins. Bertolotti also describes more recent work demonstrating that protein phosphatases are split enzymes with a catalytic subunit and a subunit that determines substrate specificity. This selective subunit makes phosphatases exquisitely specific and attractive targets for drug development.
View the full talk with additional resources on our website
Protein Phosphatases
Kinases and phosphatases perform a balancing act in cells by adding and removing phosphate groups from proteins. Dr. Bertolotti shows us that inhibiting specific protein phosphatases can reduce misfolded protein accumulation and reduce neurodegenerative disease. (Talk recorded in January 2019)
- Part 1: A Historical Perspective on Protein PhosphatasesAudience:
- Student
- Researcher
- Educators of H. School / Intro Undergrad
- Educators of Adv. Undergrad / Grad
Duration: 00:29:15 - Part 2: Benefits of Phosphatase Inhibition for Neurodegenerative DiseasesAudience:
- Researcher
- Educators of Adv. Undergrad / Grad
Duration: 00:30:12 - Part 3: A Platform to Identify Selective Protein Phosphatase InhibitorsAudience:
- Researcher
- Educators of Adv. Undergrad / Grad
Duration: 00:34:15