Asset Details
Do you wish to reserve the book?
SDS22 selectively recognizes and traps metal-deficient inactive PP1
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
SDS22 selectively recognizes and traps metal-deficient inactive PP1
Do you wish to request the book?
SDS22 selectively recognizes and traps metal-deficient inactive PP1
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
SDS22 selectively recognizes and traps metal-deficient inactive PP1
2019
Overview
The metalloenzyme protein phosphatase 1 (PP1), which is responsible for ≥50% of all dephosphorylation reactions, is regulated by scores of regulatory proteins, including the highly conserved SDS22 protein. SDS22 has numerous diverse functions, surprisingly acting as both a PP1 inhibitor and as an activator. Here, we integrate cellular, biophysical, and crystallographic studies to address this conundrum. We discovered that SDS22 selectively binds a unique conformation of PP1 that contains a single metal (M2) at its active site, i.e., SDS22 traps metal-deficient inactive PP1. Furthermore, we showed that SDS22 dissociation is accompanied by a second metal (M1) being loaded into PP1, as free metal cannot dissociate the complex and M1-deficient mutants remain constitutively trapped by SDS22. Together, our findings reveal that M1 metal loading and loss are essential for PP1 regulation in cells, which has broad implications for PP1 maturation, activity, and holoenzyme subunit exchange.
Publisher
National Academy of Sciences
Subject
/ Biophysics and Computational Biology
/ Metals
/ Nuclear Proteins - chemistry
/ Nuclear Proteins - metabolism
/ Phosphoprotein Phosphatases - chemistry
/ Phosphoprotein Phosphatases - metabolism
/ Protein Phosphatase 1 - chemistry
/ Protein Phosphatase 1 - metabolism
/ Proteins
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - growth & development
/ Saccharomyces cerevisiae - metabolism
