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Secreted kinase phosphorylates extracellular proteins that regulate biomineralization.

ABSTRACT: 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.

SUBMITTER: Tagliabracci VS

PROVIDER: S-EPMC3754843 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature

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Secreted kinase phosphorylates extracellular proteins that regulate biomineralization.

Tagliabracci Vincent S VS Engel James L JL Wen Jianzhong J Wiley Sandra E SE Worby Carolyn A CA Kinch Lisa N LN Xiao Junyu J Grishin Nick V NV Dixon Jack E JE

Science (New York, N.Y.) 20120510 6085

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 biomineraliz ...[more]

PMID: 22582013

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