TY - JOUR
T1 - Secreted protein kinases
AU - Tagliabracci, Vincent S.
AU - Pinna, Lorenzo A.
AU - Dixon, Jack E.
N1 - Funding Information:
Supported in part by National Institutes of Health (NIH) grants DK018849-36 and DK018024-37 (to J.E.D.), NIH/National Cancer Institute Training grant T32 CA009523 (to V.S.T.) and AIRC (Associazione Italiana per la Ricerca sul Cancro) grant IG-10312 (to L.A.P.). We thank Claudia Dixon and Carolyn Worby for insightful discussions regarding the manuscript. We would also like to apologize to colleagues whose work we were not able to cite owing to space constraints.
PY - 2013/3
Y1 - 2013/3
N2 - Protein kinases constitute one of the largest gene families and control many aspects of cellular life. In retrospect, the first indication for their existence was reported 130 years ago when the secreted protein, casein, was shown to contain phosphate. Despite its identification as the first phosphoprotein, the responsible kinase has remained obscure. This conundrum was solved with the discovery of a novel family of atypical protein kinases that are secreted and appear to phosphorylate numerous extracellular proteins, including casein. Fam20C, the archetypical member, phosphorylates secreted proteins within Ser-x-Glu/pSer motifs. This discovery has solved a 130-year-old mystery and has shed light on several human disorders of biomineralization.
AB - Protein kinases constitute one of the largest gene families and control many aspects of cellular life. In retrospect, the first indication for their existence was reported 130 years ago when the secreted protein, casein, was shown to contain phosphate. Despite its identification as the first phosphoprotein, the responsible kinase has remained obscure. This conundrum was solved with the discovery of a novel family of atypical protein kinases that are secreted and appear to phosphorylate numerous extracellular proteins, including casein. Fam20C, the archetypical member, phosphorylates secreted proteins within Ser-x-Glu/pSer motifs. This discovery has solved a 130-year-old mystery and has shed light on several human disorders of biomineralization.
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U2 - 10.1016/j.tibs.2012.11.008
DO - 10.1016/j.tibs.2012.11.008
M3 - Review article
C2 - 23276407
AN - SCOPUS:84874244868
SN - 0968-0004
VL - 38
SP - 121
EP - 130
JO - Trends in biochemical sciences
JF - Trends in biochemical sciences
IS - 3
ER -