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Functions of Fos phosphorylation in bone homeostasis, cytokine response and tumourigenesis

BAKIRI, L ; RESCHKE, M. O ; GEFROH, H. A ; IDARRAGA, M. H ; POLZER, K ; ZENZ, R ; SCHETT, G ; WAGNER, E. F

Oncogene, 2011-03, Vol.30 (13), p.1506-1517 [Periódico revisado por pares]

Basingstoke: Nature Publishing Group

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Título:
Functions of Fos phosphorylation in bone homeostasis, cytokine response and tumourigenesis
Autor: BAKIRI, L ; RESCHKE, M. O ; GEFROH, H. A ; IDARRAGA, M. H ; POLZER, K ; ZENZ, R ; SCHETT, G ; WAGNER, E. F
Assuntos: Alanine ; Animals ; Aspartic acid ; Biological and medical sciences ; Bone and Bones - metabolism ; Bone cancer ; Bone Remodeling ; Bone turnover ; c-Fos protein ; Carcinogenesis ; Cell Differentiation ; Cell physiology ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; Cell Transformation, Neoplastic - metabolism ; Cells, Cultured ; Cytokines ; Cytokines - biosynthesis ; Fos protein ; Fra1 protein ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation ; Genetic aspects ; Homeostasis ; Homeostasis - physiology ; Lipopolysaccharides ; Mice ; Mice, Inbred C57BL ; Molecular and cellular biology ; Mutants ; Oncology ; Osteoclastogenesis ; Osteoclasts - cytology ; Osteopetrosis ; Papilloma ; Phosphorylation ; Phosphoserine - metabolism ; Physiological aspects ; Proteins ; Proto-Oncogene Proteins c-fos - physiology ; Ribosomal protein S6 kinase ; Rodents ; Serine ; Skeletogenesis ; Skin Neoplasms - etiology ; Tumorigenesis ; Tumors
É parte de: Oncogene, 2011-03, Vol.30 (13), p.1506-1517
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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Descrição: Mice lacking c-fos develop osteopetrosis due to a block in osteoclast differentiation. Carboxy-terminal phosphorylation of Fos on serine 374 by ERK1/2 and serine 362 by RSK1/2 regulates Fos stability and transactivation potential in vitro. To assess the physiological relevance of Fos phosphorylation in vivo, serine 362 and/or serine 374 was replaced by alanine (Fos362A, Fos374A and FosAA) or by phospho-mimetic aspartic acid (FosDD). Homozygous mutants were healthy and skeletogenesis was largely unaffected. Fos C-terminal phosphorylation, predominantly on serine 374, was found important for osteoclast differentiation in vitro and affected lipopolysaccharide (LPS)-induced cytokine response in vitro and in vivo. Importantly, skin papilloma development was delayed in FosAA, Fos362A and Rsk2-deficient mice, accelerated in FosDD mice and unaffected in Fos374A mutants. Furthermore, the related Fos protein and putative RSK2 target Fra1 failed to substitute for Fos in papilloma development. This indicates that phosphorylation of serines 362 and 374 exerts context-dependent roles in modulating Fos activity in vivo. Inhibition of Fos C-terminal phosphorylation on serine 362 by targeting RSK2 might be of therapeutic relevance for skin tumours.
Editor: Basingstoke: Nature Publishing Group
Idioma: Inglês

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Functions of Fos phosphorylation in bone homeostasis, cytokine response and tumourigenesis

BAKIRI, L ; RESCHKE, M. O ; GEFROH, H. A ; IDARRAGA, M. H ; POLZER, K ; ZENZ, R ; SCHETT, G ; WAGNER, E. F

Basingstoke: Nature Publishing Group

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