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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The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity.
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: 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.
The Src Homology 2 Containing Inositol 5′ Phosphatases
Evidence of SHIP2 Ser132 phosphorylation, its nuclear localization and stability.
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.
SHIP2 signalling at the plasma membrane, in the nucleus and at focal contacts.
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.
The SHIP2 interactor Myo1c is required for cell migration in 1321 N1 glioblastoma cells.
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.
The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner.
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References

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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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