A site-specific phosphorylation of the focal adhesion kinase controls the formation of spheroid cell clusters.
Human dental follicle cells (DFCs) are ectomesenchymal multipotent stem cells that form spheroid cell clusters (SCCs) under serum free medium cell culture conditions (SFM). Until today, molecular mechanisms for the formation of SCCs are unknown. In this study a quantitative phosphoproteomics approach revealed regulated phosphorylated proteins in SCCs, which were derived from DFCs after 24 and 48 h in SFM. These regulated proteins were categorized using the Kyoto encyclopedia of genes and genomes program. Here, cellular processes and signaling pathway were identified such as the focal adhesion kinase (FAK) signaling pathway. In addition to the phosphoproteomics approach we showed that a specific phosphorylation of FAK (Y397) was required for the formation of SCCs. In conclusion, this study disclosed the phosphoproteome of SCCs for the first time and showed that the FAK signaling pathway is required for the formation of SCCs.
Department of Clinical Biochemistry and Pharmacology, Centre for Clinical Proteomics, Odense University Hospital, Sdr, Boulevard 29, 5000, Odense, Denmark.
Hans Christian
HC
Beck
Martin
M
Gosau
Lars Peter
LP
Kristensen
Christian
C
Morsczeck
D002478:Cells, Cultured; D003795:Dental Sac / Q000166:cytology / Q000201:enzymology; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation / Q000502:physiology; D018874:Spheroids, Cellular / Q000201:enzymology*
D051416:Focal Adhesion Protein-Tyrosine Kinases