SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF

@article{Xie2008SHIP2AW,
  title={SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF},
  author={Jingwei Xie and Isabelle Vandenbroere and Isabelle Pirson},
  journal={FEBS Letters},
  year={2008},
  volume={582}
}
Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits.
Protein phosphatase 2A PR130/B”α:1 subunit binds to the SH2 domain‐containing inositol polyphosphate 5‐phosphatase 2 and prevents epidermal growth factor (EGF)‐induced EGF receptor degradation sustaining EGF‐mediated signaling
TLDR
A novel biological role of the PP2AT130 holoenzyme in EGF signaling through interaction with EGFR and the phosphatidylinositol‐trisphosphate 5‐phosphatase SHIP2 is highlighted.
SHIP2 multiple functions: A balance between a negative control of PtdIns(3,4,5)P3 level, a positive control of PtdIns(3,4)P2 production, and intrinsic docking properties
TLDR
Non‐catalytic properties associated to a PI phosphatase have also been reported for other enzymes of the metabolism of myo‐inositol such as Ins(1,4,5)P3 3‐kinases, inositol phosphate multikinase (IPMK), or PTEN.
How does SHIP1/2 balance PtdIns(3,4)P2 and does it signal independently of its phosphatase activity?
TLDR
Recent interest in PtdIns(3,4)P2 signaling is discussed highlighting its involvement in key cellular mechanisms such as cell adhesion, migration, and cytoskeletal regulation.
SHIP2 controls plasma membrane PI(4,5)P2 thereby participating in the control of cell migration in 1321 N1 glioblastoma cells
TLDR
A new role is revealed of SHIP2 in the control of PI(4,5)P2, PI4P and cell migration in PTEN-deficient glioblastoma 1321 N1 cells through the organization of focal adhesions.
SHIP2: Structure, Function and Inhibition
TLDR
Inhibitors of SHIP2 activity have been designed to interact with the catalytic domain with sub‐micromolar IC50 values: these come from a range of structural classes and have been shown to have in vivo effects consistent withSHIP2 inhibition.
Aβ modulates actin cytoskeleton via SHIP2-mediated phosphoinositide metabolism
TLDR
The results provide a novel molecular link between Aβ and actin disruption through dysregulated phosphoinositide metabolism, and the SHIP2-PI(3,4)P2-ARAP3-RhoA signaling pathway can be considered as new therapeutic targets for synaptic dysfunctions in Alzheimer’s disease.
The SHIP2 interactor Myo1c is required for cell migration in 1321 N1 glioblastoma cells.
...
1
2
3
4
...

References

SHOWING 1-10 OF 27 REFERENCES
The association between the SH2‐containing inositol polyphosphate 5‐Phosphatase 2 (SHIP2) and the adaptor protein APS has an impact on biochemical properties of both partners
TLDR
It is shown that SHIP2 can directly interact with APS in 3T3‐L1 adipocytes and intransfected CHO‐IR cells (Chinese hamster ovary cells stably transfected with the insulin receptor), and it is observed thatSHIP2 negatively regulates APS insulin‐induced tyrosine phosphorylation and consequently inhibits APS association with c‐Cbl.
SHIP2 interaction with the cytoskeletal protein Vinexin
TLDR
The data reinforce the concept that SHIP2 is active both as a PtdIns(3,4,5)P3 5‐phosphatase and as a modulator of focal contact formation and suggest thatSHIP2 interaction with Vinexin promotes the localization of SHip2 at the periphery of the cells leaving its catalytic site intact.
SH2-Containing Inositol 5′-Phosphatase SHIP2 Associates with the p130Cas Adapter Protein and Regulates Cellular Adhesion and Spreading
TLDR
A novel interaction between SHip2 and the p130Cas adapter protein, a mediator of actin cytoskeleton organization, is described, suggesting an important role for SHIP2 in adhesion and spreading.
The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin
TLDR
It is demonstrated that filamin-dependent SHIP-2 localization critically regulates phosphatidylinositol 3 kinase signaling to the actin cytoskeleton.
Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP
TLDR
It is shown that intersectin-l functions through its DH domain as a guanine nucleotide exchange factor (GEF) for Cdc42, a critical activator of N-WASP.
SH2-containing 5′-Inositol Phosphatase, SHIP2, Regulates Cytoskeleton Organization and Ligand-dependent Down-regulation of the Epidermal Growth Factor Receptor*
TLDR
These experiments demonstrate that SHIP2 functions in the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation.
The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15
TLDR
Overexpression of Ese1 is sufficient to block clathrin‐mediated endocytosis in cultured cells, presumably through disruption of higher order protein complexes, which are assembled on the endogenous Ese2–Eps15 scaffold, which links dynamin, epsin and other endocytic pathway components.
The SH2 domain containing inositol 5-phosphatase SHIP2 controls phosphatidylinositol 3,4,5-trisphosphate levels in CHO-IR cells stimulated by insulin.
TLDR
It is shown that SHIP2, which is recruited in anti-phosphotyrosine immunoprecipitates in insulin-stimulated cells, accounts for the insulin sensitivity or apparent increase in activity reported by Guilherme et al.
Intersectin Can Regulate the Ras/MAP Kinase Pathway Independent of Its Role in Endocytosis*
TLDR
Intersectin SH3 domain overexpression can effect EGF-mediated MAP kinase activation directly through a block in Ras, consistent with a functional role for intersectin in Ras activation.
...
1
2
3
...