Secreted kinase phosphorylates extracellular proteins that regulate biomineralization

Vincent S. Tagliabracci, James L. Engel, Jianzhong Wen, Sandra E. Wiley, Carolyn A. Worby, Lisa N. Kinch, Junyu Xiao, Nick V. Grishin, Jack E. Dixon

Research output: Contribution to journalArticlepeer-review

352 Scopus citations


Protein phosphorylation is a fundamental mechanism regulating nearly every aspect of cellular life. Several secreted proteins are phosphorylated, but the kinases responsible are unknown. We identified a family of atypical protein kinases that localize within the Golgi apparatus and are secreted. Fam20C appears to be the Golgi casein kinase that phosphorylates secretory pathway proteins within S-x-E motifs. Fam20C phosphorylates the caseins and several secreted proteins implicated in biomineralization, including the small integrin-binding ligand, N-linked glycoproteins (SIBLINGs). Consequently, mutations in Fam20C cause an osteosclerotic bone dysplasia in humans known as Raine syndrome. Fam20C is thus a protein kinase dedicated to the phosphorylation of extracellular proteins.

Original languageEnglish (US)
Pages (from-to)1150-1153
Number of pages4
Issue number6085
StatePublished - Jun 1 2012

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Secreted kinase phosphorylates extracellular proteins that regulate biomineralization'. Together they form a unique fingerprint.

Cite this