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Rho family GTPases use the I-BAR proteins, IRSp53 (zeige BAIAP2 Proteine) (also known as BAIAP2 (zeige BAIAP2 Proteine)), IRTKS and Pinkbar (zeige BAIAP2L2 Proteine), as a central mechanism to modulate cell morphology.
IRTKS promoted serum-induced cell migration along with enhanced phosphorylation of mitogen activated kinases Erk1/2 and p38 (zeige CRK Proteine), and activation of small GTPases Rac1 and Cdc42 (zeige CDC42 Proteine). In addition, cells overexpressing IRTKS exhibited an increased polarity characterized by elongated cytoplasm and extensive lamellipodia at leading edges.
Upregulation of BAIAP2L1 is associated with ovarian cancer.
Lacking the Bin-Amphiphysin (zeige AMPH Proteine)-Rvs (BAR) dimerization domain of BAIAP2L1.
IRTKS can interact with epidermal growth factor receptor (EGFR (zeige EGFR Proteine)), results in the phosphorylation of extracellular signal-regulated kinase
Identification of a novel oncogenic FGFR3 (zeige FGFR3 Proteine)-BAIAP2L1 fusion protein in bladder cancer.
These data suggest that IRTKS is a novel regulator of p53 (zeige TP53 Proteine), modulating low level of MDM2 (zeige MDM2 Proteine)-mediated p53 (zeige TP53 Proteine) ubiquitination in unstressed cells.
data suggest Src (zeige SRC Proteine)-stimulated IRTKS phosphorylation is essential for its function in cell motility
Results describe the NMR structure of insulin receptor tyrosine kinase substrate (IRTKS) SH3 domain in complex with a repeat from Escherichia coli-secreted protein F-like protein encoded on prophage U (EspF(U)).
Study characterised IRTKS, which has widespread tissue distribution, is a substrate for the insulin receptor and binds Rac, and expression of IRTKS induces clusters of short actin bundles rather than filopodia-like protrusions.
The IRTKS, as an adaptor of the insulin receptor (IR (zeige INSR Proteine)), modulates IR-IRS1 (zeige IRS1 Proteine)-PI3K-AKT (zeige AKT1 Proteine) signaling via regulating the phosphorylation of IR.
IRTKS functions as a negative modulator of excessive inflammation in viral infections.
This gene encodes a member of the IMD (IRSp53/MIM homology domain) family. Members of this family can be subdivided in two groups, the IRSp53-like and MIM-like, based on the presence or absence of the SH3 (Src homology 3) domain. The protein encoded by this gene contains a conserved IMD, also known as F-actin bundling domain, at the N-terminus, and a canonical SH3 domain near the C-terminus, so it belongs to the IRSp53-like group. This protein is the substrate for insulin receptor tyrosine kinase and binds to the small GTPase Rac. It is involved in signal transduction pathways that link deformation of the plasma membrane and remodeling of the actin cytoskeleton. It also promotes actin assembly and membrane protrusions when overexpressed in mammalian cells, and is essential to the formation of a potent actin assembly complex during EHEC (Enterohemorrhagic Escherichia coli) pedestal formation.
BAI1-associated protein 2-like 1
, insulin receptor tyrosine kinase substrate homolog
, insulin receptor tyrosine kinase substrate
, brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1-like
, BAI1-associated protein 2-like protein 1
, brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1