The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity.

@article{Xie2008TheDP,
  title={The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity.},
  author={Jingwei Xie and Sheela Onnockx and Isabelle Vandenbroere and Chantal Degraef and Christophe Erneux and Isabelle Pirson},
  journal={Cellular signalling},
  year={2008},
  volume={20 8},
  pages={
          1432-41
        }
}
SHIP2 (SH2-containing inositol polyphosphate 5-phosphatase 2) is an ubiquitously expressed phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P(3)) 5-phosphatase which contains various motifs susceptible to mediate protein-protein interaction. In cell models, evidence has been provided that SHIP2 plays a role in insulin and growth factor signaling, cytoskeletal organization, cell adhesion and migration. Herein we describe the c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1) as… 
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TLDR
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TLDR
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The Host Phosphoinositide 5-Phosphatase SHIP2 Regulates Dissemination of Vaccinia Virus
TLDR
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Requirement of JIP1-Mediated c-Jun N-Terminal Kinase Activation for Obesity-Induced Insulin Resistance
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JIP1-mediated JNK activation plays a critical role in metabolic stress regulation of the JNK signaling pathway and is protected against obesity-induced insulin resistance.
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References

SHOWING 1-10 OF 66 REFERENCES
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 role of SHIP in cytokine-induced signaling.
TLDR
The properties of the three SHIPs are concentrated on, with special emphasis being placed on the role that SHIP plays in cytokine-induced signaling.
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 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.
Growth Factors and Insulin Stimulate Tyrosine Phosphorylation of the 51C/SHIP2 Protein
TLDR
The data suggest that 51C/SHIP2 may play a significant role in regulation of phosphatidylinositol 3′-kinase signaling by growth factors and insulin.
Molecular cloning of rat SH2-containing inositol phosphatase 2 (SHIP2) and its role in the regulation of insulin signaling.
TLDR
Results indicate that SHIP2 plays a negative regulatory role in insulin-induced mitogenesis, and regulation of the Shc.
SH2-containing inositol phosphatase 2 negatively regulates insulin-induced glycogen synthesis in L6 myotubes
TLDR
The results indicate that SHIP2 plays a negative regulatory role via the 5'-phosphatase activity in insulin signalling, and that PI(3,4,5)P3 rather than PI( 3,4)P2 is important for in vivo regulation of insulin-induced Akt activation leading to glycogen synthesis in L6 myotubes.
The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2.
TLDR
It is shown that SHIP2 was able to coimmunoprecipitate with endogenous c-Cbl protein in the absence of CAP and with the insulin receptor in CHO-IR cell extracts and could account for the very specific increase in insulin sensitivity ofSHIP2 knock-out mice.
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.
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