Since the discovery of protein kinases, protein phosphorylation has emerged as a key regulatory mechanism. The majority of phosphoproteins reside within the nucleus and cytoplasm; however, many secreted proteins are phosphorylated by unknown kinases located within the secretory pathway and/or in the extracellular space. The Fam20 kinases are emerging as the enzymes responsible for phosphorylating secreted proteins and proteoglycans. Evolutionary analysis reveals that these kinases are exclusively present in metazoans and contain conserved features that are common among all eukaryotic protein kinases. Mutations in the Fam20 family members cause disorders of biomineralization in humans that highlight the physiological significance of secreted protein phosphorylation.
Skip Nav Destination
Conference Article| July 18 2013
Phosphorylation of substrates destined for secretion by the Fam20 kinases
Vincent S. Tagliabracci;
Jack E. Dixon
Jack E. Dixon 2
*Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093, U.S.A.
†Howard Hughes Medical Institute, Chevy Chase, MD 20815, U.S.A.
2To whom correspondence should be addressed (firstname.lastname@example.org).
Search for other works by this author on:
- Views Icon Views
- Share Icon Share
Vincent S. Tagliabracci, Junyu Xiao, Jack E. Dixon; Phosphorylation of substrates destined for secretion by the Fam20 kinases. Biochem Soc Trans 1 August 2013; 41 (4): 1061–1065. doi: https://doi.org/10.1042/BST20130059
Download citation file:
Don't already have an account? Register
Get Access To This Article
Buy This Article