IndraLab

Statements


INS leads to the phosphorylation of SHC1. 17 / 17
1 | 1 15

sparser
"Molecules involved in mitogenic signaling such as Grb2, SHC, and MAPK have been found to co-localize with the endosomal IR ( xref ) and inhibition of IR internalization significantly reduces insulin-induced Shc and MAPK phosphorylation ( xref )."

sparser
"However, insulin-induced tyrosine phosphorylation of the insulin receptor and SHC, and the association of SHC/growth factor receptor binding protein-2 (GRB2) decreased significantly from d 1 to wk 60 of life in both types of tissues."

sparser
"In rat aortic VSMC, insulin induced rapid phosphorylation of the IR and Shc and caused a 5.3-fold increase in activated, phosphorylated ERK1/2 at 10 min."

sparser
"Although overexpression of SHIP2 did not affect insulin-induced tyrosine phosphorylation of the insulin receptor beta-subunit and Shc, subsequent association of Shc with Grb2 was inhibited, possibly by competition between the SH2 domains of SHIP2 and Grb2 for the Shc phosphotyrosine."

sparser
"The dissociation of insulin-induced IRS-1 and Shc tyrosine phosphorylation has been described in cell lines with mutations at two tyrosine phosphorylation sites (Y1158, Y1162F, Y1163F-YFF) on the insu[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"As yet, there has been no comparison of insulin-induced IRS-1 and Shc tyrosine phosphorylation in situations of insulin resistance accompanied by a reduction in insulin receptor phosphorylation."

sparser
"Thus, interference with the IRS-1-IR interaction inhibits insulin-stimulated IRS-1 and Shc phosphorylation, PI 3-K enzymatic activity, p70s6k activation, MAPK phosphorylation and cell cycle progression."

sparser
"Insulin-dependent phosphorylation of IRS1/2 and Shc was not affected by siJAK2, but insulin-induced phosphorylation of the mitogen-activated protein kinases (MAPKs) extracellular signal-related kinase, p38, and Jun NH2-terminal kinase and their respective upstream kinases MKK1/2, MKK3/6, and MKK4/7 was significantly lowered when JAK2 was depleted, correlating with a significant drop in insulin-mediated cell proliferation."

sparser
"Insulin and IGF-1 stimulated tyrosine phosphorylation of IRS-1 and Shc in a similar dose- and time-dependent manner."

sparser
"Consistent with a receptor level effect, in vivo insulin-dependent tyrosine phosphorylation of both IRS-1 and Shc was increased by a similar 3-fold with LAR suppression."

sparser
"In fat cells, insulin induces serine 36-specific phosphorylation of p66Shc, thus stimulating p66Shc ROS production, which, in turn, potentiates insulin transduction signaling by inhibiting PTEN phosph[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"However, insulin induced tyrosine phosphorylation of IR and SHC, and the association of SHC/growth factor receptor binding protein-2 (GRB2) decreased significantly in both types of tissues [ xref ]."

sparser
"In both cell types, overexpression of either the PTB or the SAIN protein caused a significant decrease in insulin-induced tyrosine phosphorylation of IRS-1 and Shc proteins, IRS-1-associated phosphatidylinositol 3-kinase (PI 3-K) enzymatic activity, p70s6k activation, and p44 and p42 mitogen-activated protein kinase (MAPK) phosphorylation."

"The 52kDa isoform of Shc was phosphorylated in response to insulin or EGF stimulation."

sparser
"Reconstitution of IRS-1-deficient brown adipocytes with wild-type IRS-1 restored insulin-induced IRS-1 and SHC tyrosine phosphorylation and IRS-1-Grb-2, IRS-1-SHC, and SHC-Grb-2 associations, leading to the activation of MAPK and enhancement of DNA synthesis."

reach
"In fat cells, insulin induces serine 36 specific phosphorylation of p66Shc, thus stimulating p66Shc ROS production, which, in turn, potentiates insulin transduction signaling by inhibiting PTEN phosph[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Insulin-dependent tyrosine phosphorylation of insulin receptor substrate 1 (IRS-1) and Shc was 3-fold greater in CD45- cells."