Asset Details
Do you wish to reserve the book?
The growing landscape of lysine acetylation links metabolism and cell signalling
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?
The growing landscape of lysine acetylation links metabolism and cell signalling
Do you wish to request the book?
The growing landscape of lysine acetylation links metabolism and cell signalling
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
The growing landscape of lysine acetylation links metabolism and cell signalling
2014
Overview
Key Points
Advances in mass spectrometry-based proteomics have enabled the global identification and characterization of thousands of acetylation sites, ushering in the age of acetylomics.
Acetylation intersects with cellular metabolism at multiple levels: metabolic intermediates regulate acetyltransferases and deacetylases, acetylation can affect metabolic pathways, and metabolites may directly acetylate proteins through non-enzymatic mechanisms.
Acetylation regulates protein function by affecting protein interactions with nucleic acids and with other proteins, the catalytic activity of proteins, and protein localization.
Emerging data indicate that other types of acylations, such as succinylation and glutarylation, are also linked to metabolic activity and are regulated by sirtuin-class deacylases.
Recent technical advances are expanding our understanding of how lysine acetylation, as well as other metabolite-sensitive acylations, regulates various cellular processes. Emerging findings point to new functions for different acylations and deacylating enzymes, and clarify the intricate link between lysine acetylation and cellular metabolism.
Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased our understanding of lysine acetylation, implicating it in many biological processes through the regulation of protein interactions, activity and localization. In addition, proteins are frequently modified by other types of acylations, such as formylation, butyrylation, propionylation, succinylation, malonylation, myristoylation, glutarylation and crotonylation. The intricate link between lysine acylation and cellular metabolism has been clarified by the occurrence of several such metabolite-sensitive acylations and their selective removal by sirtuin deacylases. These emerging findings point to new functions for different lysine acylations and deacylating enzymes and also highlight the mechanisms by which acetylation regulates various cellular processes.
Publisher
Nature Publishing Group UK,Nature Publishing Group
