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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.
SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF
TLDR
Physically interacts with SHIP2 (uniprotkb:O15357) by anti tag coimmunoprecipitation (MI:0007).
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.
The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity.
TLDR
The c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1) is described as a new protein partner of SHIP2 and data suggest that by its docking properties,SHIP2 can modulate JIP1-mediated JNK pathway signaling.
Endogenous SHIP2 does not localize in lipid rafts in 3T3‐L1 adipocytes
TLDR
This two‐hybrid study showed that SHIP2 interacts with c‐Cbl associated protein (CAP) and c-Cbl, implicated in the insulin signaling, and demonstrated that SHip2 acts as a negative regulator of insulin cascade in vivo.
Interpretation of low-copy-number DNA profile after post-PCR purification
TLDR
A multiple PCR strategy with post-PCR purification is used to help interpret low-copy-number DNA profile and careful interpretation of peaks present at a stutter position is necessary.
Use of two-hybrid methodology for identifying proteins of interest in endocrinology
TLDR
The contribution of the two-hybrid technique already is and will be essential in dissecting the molecular mechanism of transduction pathways in many cell types.
IRSp53 is a novel interactor of SHIP2: A role of the actin binding protein Mena in their cellular localization in breast cancer cells.
TLDR
The data suggest that SHIP2, through interaction with the cell protrusion regulators IRSp53 and Mena, participate to the formation of multi-protein complexes, which ensures the appropriate modulations of PIs which is important for regulation of membrane dynamics.