Challenges of assigning protein kinases to in vivo phosphorylation events. Focus on "Use of LC-MS/MS and Bayes' theorem to identify protein kinases that phosphorylate aquaporin-2 at Ser256"

Prihandoko, R. and Tobin, A. B. (2014) Challenges of assigning protein kinases to in vivo phosphorylation events. Focus on "Use of LC-MS/MS and Bayes' theorem to identify protein kinases that phosphorylate aquaporin-2 at Ser256". American Journal of Physiology: Cell Physiology, 307(2), C121-C122. (doi: 10.1152/ajpcell.00136.2014) (PMID:24829494)

Abstract

reversible phosphorylation plays an important role in regulating the functions of many cellular proteins. This posttranslational modification acts as a molecular switch to turn proteins on and off in an acute and transient manner (4). Although there have been major advances in recent years in mass spectrometry-based proteomics to evaluate and quantify phosphoproteins in complex samples (3), this area presents significant challenges. It is in this context that Bradford et al. (2) report in this issue of American Journal of Physiology-Cell Physiology their work describing the protein kinases that potentially phosphorylate a key residue (Ser256) in aquaporin-2, a protein expressed in renal inner medullary collecting duct (IMCD) cells, which regulate water transport and renal water excretion. Although Ser256 is among four COOH-terminal sites that are phosphorylated in aquaporin-2 in response to the action of vasopressin on renal collecting duct cells, this phosphorylation event is thought to be key in controlling the trafficking of aquaporin-2 to the apical membrane of those cells and in regulating other phosphorylation events in the COOH-terminal tail. Bradford et al. employed bioinformatics, together with protein kinase inhibitors and mass spectrometry-based phosphoproteomics, to determine the potential protein kinases that phosphorylate aquaporin-2 on Ser256.

• Item Type: Articles (Editorial)
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Prihandoko, Dr Rudi and Tobin, Andrew
• Authors: Prihandoko, R., and Tobin, A. B.
• College/School: College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
• Journal Name: American Journal of Physiology: Cell Physiology
• Publisher: American Physiological Society
• ISSN: 0363-6143
• ISSN (Online): 1522-1563