SHIP2 interaction with the cytoskeletal protein Vinexin

@article{Paternotte2005SHIP2IW,
  title={SHIP2 interaction with the cytoskeletal protein Vinexin},
  author={Nathalie Paternotte and Jing Zhang and Isabelle Vandenbroere and Katrien Backers and Daniel Bl{\'e}ro and Noriyuki Kioka and Jean-Marie Vanderwinden and Isabelle Pirson and Christophe Erneux},
  journal={The FEBS Journal},
  year={2005},
  volume={272}
}
The src homology 2 (SH2) domain‐containing inositol 5‐phosphatase 2 (SHIP2) catalyses the dephosphorylation of phosphatidylinositol 3,4,5‐trisphosphate [PtdIns(3,4,5)P3] to phosphatidylinositol 3,4‐bisphosphate [PtdIns(3,4)P2]. We report the identification of the cytoskeletal protein Vinexin as a protein interacting with SHIP2. This was achieved by yeast two‐hybrid screening using the C‐terminal region of SHIP2 as bait. Vinexin has previously been identified as a vinculin‐binding protein that… 
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TLDR
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TLDR
It is suggested that the function of SHIP2 is different at the plasma membrane where it recognizes PtdIns(3,4,5)P3, and in the nucleus where it may interact with PTDIns(4, 5)P2, particularly in speckles.
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TLDR
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The SHIP2 interactor Myo1c is required for cell migration in 1321 N1 glioblastoma cells.
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TLDR
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References

SHOWING 1-10 OF 51 REFERENCES
Phosphatidylinositol 3,4,5‐trisphosphate modulation in SHIP2‐deficient mouse embryonic fibroblasts
TLDR
A link between SHIP2 and the acute control of PtdIns(3,4,5)P3 levels in intact cells is established and it is shown that this lipid was significantly upregulated in ShIP2 –/– cells but only after short‐term incubation with serum.
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.
Vinexin: A Novel Vinculin-binding Protein with Multiple SH3 Domains Enhances Actin Cytoskeletal Organization
TLDR
Using the yeast two-hybrid system and an in vitro binding assay, vinexin is identified as a novel focal adhesion and cell– cell adhesion protein that binds via SH3 domains to the hinge region of vinculin, which can enhance actin cytoskeletal organization and cell spreading.
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.
SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: their interactions and roles in the control of phosphatidylinositol 3,4,5-trisphosphate levels.
TLDR
The results strongly suggest that SHIP1, rather than SHIP2, plays a major role in controlling PtdIns(3,4,5) P3 levels in response to thrombin or collagen activation of mouse blood platelets.
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 Src Homology 2 Domain Containing Inositol 5-Phosphatase SHIP2 Is Recruited to the Epidermal Growth Factor (EGF) Receptor and Dephosphorylates Phosphatidylinositol 3,4,5-Trisphosphate in EGF-stimulated COS-7 Cells*
TLDR
It is shown that upon stimulation by EGF, phosphatidylinositol 3,4,5-trisphosphate and protein kinase B activity were decreased in SHIP2-transfected COS-7 cells as compared with the vector alone.
The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met directly via tyrosine residue 1356 and involves hepatocyte growth factor (HGF)-induced lamellipodium formation, cell scattering and cell spreading
TLDR
It is shown for the first time that the SH2-domain-containing inositol 5-phosphatase (SHIP)-2 binds directly to the hepatocyte growth factor (HGF/SF) receptor, c-Met, via phosphotyrosine 1356, suggesting that a balance between PI3 kinase and SHIP is important for cell motility.
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