Secreted kinase phosphorylates extracellular proteins that regulate biomineralization |
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Authors: | Tagliabracci Vincent S Engel James L Wen Jianzhong Wiley Sandra E Worby Carolyn A Kinch Lisa N Xiao Junyu Grishin Nick V Dixon Jack E |
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Institution: | Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0721, USA. |
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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. |
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