FAM20C functions intracellularly within both ameloblasts and odontoblasts in vivo.

ABSTRACT: FAM20C, also known as Golgi casein kinase (G-CK), is proposed to be the archetype for a family of secreted kinases that phosphorylate target proteins in the Golgi and in extracellular matrices, but FAM20C serving an extracellular function is controversial. FAM20C phosphorylates secretory calcium-binding phosphoproteins (SCPPs), which are associated with the evolution of biomineralization in vertebrates. Current models of biomineralization assume SCPP proteins are secreted as phosphoproteins and their phosphates are essential for protein conformation and function. It would be a radical departure from current theories if proteins in mineralizing matrices were dephosphorylated as part of the mineralization mechanism and rephosphorylated in the extracellular milieu by FAM20C using ATP. To see

SUBMITTER: Wang SK 

PROVIDER: S-EPMC3836880 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature