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CSF1 — SOAT1
Text-mined interactions from Literome
Novak et al., Blood 1995
:
Furthermore, we propose that kinases other than JAK kinase may be involved in the phosphorylation of the
STAT proteins in
response to
CSF-1
Novak et al., Oncogene 1996
:
Using FDC-P1 derived cell lines which ectopically express either the wild type or mutant forms of the murine CSF-1 receptor in which individual tyrosine residues have been replaced with phenylalanine, we analysed the requirement for tyrosine residues of the receptor for the activation of
STAT proteins in
response to
CSF-1 ... Replacement of Y807 with phenylalanine led to a complete block of activation of all
STAT proteins in
response to
CSF-1 , however, this phosphotyrosine does not appear to represent a STAT binding site of the receptor as a phosphopeptide spanning Y809 of the human CSF-1 receptor could not compete any STAT/DNA complex formation in electrophoretic mobility shift assays
Novak et al., Growth Factors 1998
:
CSF-1 causes the activation of
STAT proteins in FDwtfms cells, but not in 807F cells
Hamilton et al., Int J Biochem Cell Biol 1998
:
In contrast to some other growth factor/cell systems, no evidence was obtained using the inhibitors for the involvement of PI3-kinase or p70s6k in CSF-1 mediated induction of c-fos mRNA expression or Erk-1 activity ; in addition, no evidence was found for an involvement in the
CSF-1 mediated
increase in cyclin D1 expression or
STAT activation