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AKT3 — CSF1

Text-mined interactions from Literome

Kelley et al., J Biol Chem 1999 : To clarify that PI3K products activate Akt in response to M-CSF , NIH 3T3 fibroblasts expressing mutant human M-CSF receptors ( 3T3-FMS ( Y809F ) ) that fail to activate Ras in response to M-CSF also exhibit increased Akt kinase activity in response to M-CSF challenge ... In normal human monocytes, M-CSF increased the levels of tyrosine phosphorylated proteins and induced Akt activation in a PI3K dependent manner
Murray et al., Inflamm Res 2000 : Stimulation of BAC1.2F5 macrophages with M-CSF induced phosphorylation of PKB/Akt as detected by activation-specific antibodies
Baran et al., J Biol Chem 2003 : Because the inositol 5'-phosphatase SHIP-1 is an important regulator of intracellular levels of phosphatidylinositol 3,4,5-trisphosphate, an important second messenger necessary for Akt activation, we hypothesized that SHIP-1 was involved in the regulation of M-CSF receptor (M-CSF-R) induced Akt activation ... Transfection of 3T3-Fms cells, which express the human M-CSF-R, with wild-type SHIP-1 showed that SHIP-1 was necessary for the negative regulation of M-CSF induced Akt activation ... These data provide the first evidence of the involvement of both SHIP-1 and Lyn in the negative regulation of M-CSF-R induced Akt activation
Kwak et al., Biochem Pharmacol 2004 (Bone Resorption) : M-CSF and RANKL activate the ERK, Akt , and NF-kappaB signal transduction pathways, and SCOH suppressed this activation
Wang et al., J Immunol 2004 : Analyzing the function of SHIP2 in M-CSF stimulated cells by expressing either wild-type SHIP2 or an Src homology 2 domain mutant of SHIP2 reduced Akt activation in response to M-CSF stimulation
Manes et al., FEBS J 2006 : Overexpression of SLAP-2 in bone marrow macrophages partially suppressed the CSF-1 induced tyrosine phosphorylation and/or expression level of a approximately 80 kDa protein without affecting CSF-1 induced global tyrosine phosphorylation, or activation of Akt or Erk1/2
Yang et al., J Clin Invest 2006 (Bone Resorption...) : M-CSF stimulated p21(ras)-GTP and Akt phosphorylation was elevated in Nf1 ( +/- ) osteoclasts associated with gains of function in survival, proliferation, migration, adhesion, and lytic activity
Ikeda et al., Biochem Biophys Res Commun 2007 : Ectopic expression of STAP-2 markedly suppressed M-CSF induced tyrosine phosphorylation of c-Fms as well as activation of Akt and extracellular signal regulated kinase
Guillermet-Guibert et al., Proc Natl Acad Sci U S A 2008 : In macrophages, both p110beta and p110gamma contributed to Akt activation induced by the GPCR agonist complement 5a, but not by the Tyr kinase ligand colony stimulating factor-1
Jacquel et al., Blood 2009 : CSF-1 and its receptor are both required for oscillations in AKT activation to occur, and expression of a constitutively active AKT mutant prevents the macrophage differentiation process
Mandal et al., Endocrinology 2009 : Inhibition of PI3K/Akt signaling blocked the binding of Smads 1/5 to the CSF-1 BMP-responsive element present in the CSF-1 promoter, resulting in attenuation of Smad dependent CSF-1 transcription ... Together, these data for the first time demonstrate that PI3K dependent Akt activation regulates BMP-2 induced CSF-1 expression and provides a mechanism for osteoblastic cell assisted osteoclast differentiation
Gueller et al., J Leukoc Biol 2010 : Furthermore, the M-CSF induced phosphorylation of Akt in Lnk KO macrophages was increased and prolonged, whereas phosphorylation of Erk was diminished
Zwaenepoel et al., FASEB J 2012 (Breast Neoplasms) : In response to CSF-1 , added to intact cells or isolated nuclei, nucleus associated CSF-1R became phosphorylated and triggered the phosphorylation of Akt and p27 inside the nucleus