Phosphorylation of substrates destined for secretion by the Fam20 kinases

Vincent S. Tagliabracci, Junyu Xiao, Jack E. Dixon

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Since the discovery of protein kinases, protein phosphorylation has emerged as a key regulatory mechanism. The majority of phosphoproteins reside within the nucleus and cytoplasm; however, many secreted proteins are phosphorylated by unknown kinases located within the secretory pathway and/or in the extracellular space. The Fam20 kinases are emerging as the enzymes responsible for phosphorylating secreted proteins and proteoglycans. Evolutionary analysis reveals that these kinases are exclusively present in metazoans and contain conserved features that are common among all eukaryotic protein kinases. Mutations in the Fam20 family members cause disorders of biomineralization in humans that highlight the physiological significance of secreted protein phosphorylation.

Original languageEnglish (US)
Pages (from-to)1061-1065
Number of pages5
JournalBiochemical Society Transactions
Volume41
Issue number4
DOIs
StatePublished - Aug 1 2013

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Keywords

  • Amelogenesis imperfecta
  • Fam20A
  • Fam20B
  • Fam20C
  • Hypophosphataemia
  • Raine syndrome

ASJC Scopus subject areas

  • Biochemistry

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