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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]

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