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INS — STK31
Text-mined interactions from Literome
Li et al., J Biol Chem 1999
:
In addition, the PDGF activated
serine/threonine kinase called Akt was found to
inhibit insulin signaling
Tartare et al., J Biol Chem 1991
:
These results suggest that
insulin-EGF chimeric receptor activation
stimulates at least one
serine/threonine kinase , which in turn phosphorylates the kinase-deficient EGF receptor
Izumi et al., J Biol Chem 1991
:
We have examined the phosphorylation of the
serine threonine kinase , the product of c-raf proto-oncogene in
response to
insulin or platelet derived growth factor in intact cells
Shaw et al., Cell Metab 2008
(Muscular Dystrophies) :
The mammalian target of rapamycin (mTOR)
serine/threonine kinase plays a central role in
insulin signaling and cell growth, through two distinct complexes with its subunits raptor or rictor
Amato et al., J Mol Med (Berl) 2009
:
Serum and glucocorticoid regulated kinase 1 ( Sgk1 ) is a
serine-threonine kinase that is
activated by serum, steroids,
insulin , vasopressin, and interleukin 2 at the transcriptional and post-translational levels
Bergeron et al., Endocrinology 2011
:
Expression of DNSHP-1 increased
insulin induced Akt
serine-threonine kinase phosphorylation and augmented glucose uptake and glycogen synthesis
Kovacina et al., J Biol Chem 1990
:
These findings indicate that
insulin activates the
serine/threonine kinase activity of the Raf-1 proto-oncogene by increasing its content of phosphoserine
Yuzefovych et al., Endocrinology 2012
:
Protection of mtDNA from palmitate induced damage by overexpression of hOGG1 targeted to mitochondria significantly diminished palmitate induced mitochondrial superoxide production, restored the decline in ATP levels, reduced activation of c-Jun N-terminal kinase (JNK) kinase, prevented cells from entering apoptosis, increased
insulin stimulated phosphorylation of
serine-threonine kinase ( Akt ) ( Ser473 ) and tyrosine phosphorylation of insulin receptor substrate-1, and thereby enhanced glucose transporter 4 translocation to plasma membrane, and restored insulin signaling
Filho et al., Eur J Pharmacol 2013
(Hypertrophy, Left Ventricular...) :
Insulin induced vasorelaxation due to endothelial nitric oxide synthase (eNOS) activation is highly dependent on the activation of the upstream
insulin stimulated
serine/threonine kinase ( AKT ) and is severely impaired in obese, hypertensive rodents and humans
Yu et al., Proc Natl Acad Sci U S A 1987
:
The
insulin stimulated
serine/threonine kinase exhibits preferential phosphorylation of histone and Kemptide ( synthetic Leu-Arg-Arg-Ala-Ser-Leu-Gly ) compared to a number of other peptide substrates ... The data suggest that this
insulin stimulated
serine/threonine kinase in adipocyte high-density microsomes is tyrosine phosphorylated, consistent with the hypothesis that the stimulatory action of insulin on this kinase may be mediated by tyrosine phosphorylation
Silliman et al., Biochem Biophys Res Commun 1989
:
Chymotryptic digestion was used to localize the sites in microtubule associated protein 2 which are preferentially phosphorylated in vitro by MAP kinase, an
insulin stimulated
serine/threonine kinase which efficiently utilizes high molecular weight MAPs as substrates
Rossomando et al., Proc Natl Acad Sci U S A 1989
:
Stimulation of 3T3-L1 cells with
insulin has been shown to
activate a cytosolic
serine/threonine kinase capable of phosphorylating microtubule associated protein 2 (MAP-2) and ribosomal protein S6 kinase II
Brownsey et al., Biochem Cell Biol 1988
:
A range of assay conditions was employed to characterize the
insulin stimulated protein
serine ( threonine ) kinase in in supernatant fractions ... The
insulin stimulated protein
serine ( threonine ) kinase displays properties that indicate it is distinct from a number of well characterized protein kinases, including those regulated by cAMP, calcium ions ( in the presence or absence of calmodulin or mixtures of phosphatidylserine-diacylglycerol ), polyamines, or heparin
Ray et al., Proc Natl Acad Sci U S A 1987
:
These results show that a soluble
serine/threonine kinase is rapidly
activated by
insulin , possibly by phosphorylation of either the kinase itself or an interacting modulator
Brozinick et al., J Biol Chem 1998
:
In the present study, we have examined the role of Akt, an
insulin activated
serine threonine kinase that has previously been shown to increase glucose transport in adipocytes