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Human Polyclonal INPPL1 Primary Antibody pour ICC, IF - ABIN151139
Yoshinaga, Ohkubo, Sasaki, Nuriya, Ogawa, Yasui, Tabata, Nakajima: A phosphatidylinositol lipids system, lamellipodin, and Ena/VASP regulate dynamic morphology of multipolar migrating cells in the developing cerebral cortex. dans The Journal of neuroscience : the official journal of the Society for Neuroscience 2012
Human Polyclonal INPPL1 Primary Antibody pour ICC, IF - ABIN4353371
Mostafavi, Gaiteri, Sullivan, White, Tasaki, Xu, Taga, Klein, Patrick, Komashko, McCabe, Smith, Bradshaw, Root, Regev, Yu, Chibnik, Schneider, Young-Pearse, Bennett, De Jager: A molecular network of the aging human brain provides insights into the pathology and cognitive decline of Alzheimer's disease. dans Nature neuroscience 2018
SHIP phosphatases control neutrophil inflammation by limiting neutrophil motility in vivo.
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.
results indicated genotype and allele frequency of SHIP2(+1893CC/AA) locus in Type 2 diabetes mellitus (T2DM) Han Chinese patients was significantly different from healthy controls; G allele (+2945A/G) seemed to increase susceptibility to hypertension for T2DM patients
Inactivation of SHIP2 leads to increased microvilli formation and solute reabsorption by the renal proximal tubule and was associated with hyperactivated ezrin/radixin/moesin proteins and increased Rho-GTP.
data suggest that endothelial SHIP2 is required to maintain normal systemic glucose homeostasis and prevent oxidative stress-induced endothelial dysfunction.
The authors concluded that the FcgammaRIIb-SHIP2 axis links Abeta neurotoxicity to tau pathology by dysregulating phosphoinositide metabolism, providing insight into therapeutic potential against Alzheimer's disease.
These findings suggest that palmitate contributes to SHIP2 overexpression in skeletal muscle via the mechanisms involving the activation of ceramide-JNK and NF-kappaB pathways.
results suggest that SHIP2 contributes to the regulation of food intake mainly via the attenuation of insulin signalling in the hypothalamus of mice
The catalytically-inactive Ship2 mutant protein in a context of reduced PtdIns(4,5)P2 3-kinase activity.
Regulation of insulin signaling and glucose transporter 4 (GLUT4) exocytosis by phosphatidylinositol 3,4,5-trisphosphate (PIP3) phosphatase, skeletal muscle, and kidney enriched inositol polyphosphate phosphatase (SKIP).
These results suggest that SHIP2 is a potent negative regulator of insulin/IGF-I actions in the brain, and excess amounts of SHIP2 may be related, at least in part, to brain dysfunction in insulin resistance with type 2 diabetes.
The SHIP2 is a negative regulator of insulin signaling, our findings suggest the importance of the phosphoinositide metabolism at endocytic clathrin-coated pits in the regulation of insulin signal output.
Association with the insulin resistance of diabetic db/db mice.
The role of SHIP2 in controlling phosphatidylinositol 3,4,5-trisphosphate levels in platelets.
SH2-containing inositol phosphatase 2 predominantly regulates Akt2, and not Akt1, phosphorylation at the plasma membrane in response to insulin in adipocytes
SHIP2 plays an important role in the negative regulation of insulin signaling for protein synthesis and the impact of SHIP2 is altered, dependent on the acute or chronic exposure of excess concentrations of amino acids in culture.
SHIP2 does not localize in lipid rafts in 3T3-L1 adipocytes
a second tyrosine-containing motif in the intracytoplasmic domain of FcgammaRIIB is required for SHIP1/2 to be coprecipitated with the receptor
Results suggest that inhibition of SHIP2 would be useful in the effort to ameliorate diet-induced obesity, but call into question a dominant role of SHIP2 in modulating glucose homeostasis.
Inhibition of endogenous SHIP2 is effective in improving the state of insulin resistance caused by chronic insulin treatment.
SHIP2 does not function as a suppressor of insulin signaling to glucose transport through the PI 3-kinase pathway in cultured 3T3-L1 adipocytes
Data establish a link between SHIP2 and the acute control of phosphatidylinositol 3,4,5-trisphosphate levels in intact cells.
a negative regulator of IgE-induced mast cell activation via a calcium-independent pathway
we suggest that SHIP2 might play a role in the regulation of skeletal muscle development in pigs
The protein encoded by this gene is an SH2-containing 5'-inositol phosphatase that is involved in the regulation of insulin function. The encoded protein also plays a role in the regulation of epidermal growth factor receptor turnover and actin remodelling. Additionally, this gene supports metastatic growth in breast cancer and is a valuable biomarker for breast cancer.
SH2-domain-containing inositol 5-phosphatase 2b
, inositol polyphosphate phosphatase-like 1
, phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2-like
, 51C protein
, SH2 domain-containing inositol 5'-phosphatase 2
, SH2 domain-containing inositol-5'-phosphatase 2
, phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
, phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
, protein 51C
, SH2 domain-containing inositol phosphatase 2
, ablSH3-binding protein
, inositol polyphosphate phosphatase-like protein 1
, SH2-containing inositol phosphatase 2