-
FBP17 and CIP4 prime the membrane of resting cells for fast endophilin-mediated endocytosis by recruiting the 5'-lipid phosphatase SHIP2 and lamellipodin to mediate the local production of phosphatidylinositol-3,4-bisphosphate and endophilin pre-enrichment.
-
Results find SHIP2 expression negatively regulated by ZIC2. Its expression is downregulated in osteosarcoma cells and tissues.
-
The authors report two novel mutations in the INPPL1 gene and show that cell migration is very much decreased in fibroblasts derived from three opsismodysplasia (OPS) patients as compared with control individuals. In contrast, cell adhesion on fibronectin is increased in OPS fibroblasts.
-
Aiming to uncover interdomain regulatory mechanisms in SHIP2, the authors determined crystal structures containing the 5-phosphatase and a proximal region adopting a C2 fold. This reveals an extensive interface between the two domains, which results in significant structural changes in the phosphatase domain.
-
the expression and intrinsic phosphatase activity of the lipid phosphatase SHIP2 is increased in human colorectal cancer, and that increased expression within a large cohort of CRC patient is correlated to a worse patient survival. SHIP2 functions as an oncogene, by enhancing cell migration and invasion, and reducing cell adhesion in colorectal cancer cells.
-
HIP2 regulates mitotic spindle alignment. SHIP2 is expressed in G1 phase, whereas Aurora A kinase is enriched in mitosis. SHIP2 binds Aurora A kinase and the scaffolding protein HEF1 and promotes their basolateral localization at the expense of their luminal expression connected with cilia resorption.
-
article focuses on the mutations associated with opsismodysplasia and explores the role of INPPL1/ SHIP2 in skeletal development (Review)
-
SHIP2 recruits Mena to invadopodia and disruption of SHIP2-Mena interaction in cancer cells leads to attenuated capacity for ECM degradation and invasion in vitro, as well as reduced metastasis in vivo.
-
In glioblastoma 1321 N1 cells, we recently identified Myo1c as a new interactor of SHIP2. SHIP2 localization at lamellipodia and ruffles is impaired in Myo1c depleted cells. In the absence of Myo1c, N1 cells tend to associate to form clusters.
-
decreased expression of transcription factor Sp1 contributes to suppression of SHIP2 in gastric cancer cells.
-
In order to shed light on the role of the C2 related (C2R) domain, immediately C-terminal to the SHIP2 phosphatase domain, molecular cloning, expression, purification and crystallization of the human SHIP2 fragment containing the phosphatase (Ptase) and C2R domains were performed an X-ray crystallographic data analysis was conducted.
-
Regulation of phosphatidylinositol 4,5-bisphosphate by SHIP2 controls glioblastoma cell migration through the organization of focal adhesions.
-
the dissociation process of the EphA2-SHIP2 SAM-SAM domain heterodimer complex the dissociation process of the EphA2-SHIP2 SAM-SAM domain heterodimer complex
-
Suppression of SHIP2 contributes to tumorigenesis and proliferation of gastric cancer cells via activation of Akt.
-
these findings suggest that SHIP2 is an important regulator of hepatic lipogenesis and lipoprotein secretion in insulin resistance state.
-
investigated the molecular link between SHIP2 expression and metabolic dyslipidemia using overexpression or suppression of SHIP2 gene in HepG2 cells
-
Findings indicate that SHIP2 is a regulator of lymphatic function in humans and that inherited mutations in the INPPL1 gene may act in concert with HGF, and likely MAP3K7, mutations to exacerbate lymphatic phenotypes.
-
SHIP2 inhibition was accompanied by an increased Akt and FOXO-1 phosphorylation, whereas overexpression of the wild-type SHIP2 gene had the opposite effects
-
In conclusion, SHIP2 plays a key role in breast cancer stem cells of ER-negative breast cancers
-
Kaplan-Meier method and Cox multifactor analysis suggested that high SHIP2 protein level and positive distant metastasis were critically associated with the unfavorable survival of coloretal cancer patients.
