INPPL1 Antibody

1. Results find SHIP2 expression negatively regulated by ZIC2. Its expression is downregulated in osteosarcoma cells and tissues. PMID: 28857346
2. 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. PMID: 28869677
3. 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. PMID: 28792888
4. 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. PMID: 27716613
5. 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. PMID: 27926875
6. article focuses on the mutations associated with opsismodysplasia and explores the role of INPPL1/ SHIP2 in skeletal development (Review) PMID: 27708270
7. 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. PMID: 27597754
8. 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. PMID: 27246739
9. decreased expression of transcription factor Sp1 contributes to suppression of SHIP2 in gastric cancer cells. PMID: 28117748
10. 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. PMID: 27170292
11. Regulation of phosphatidylinositol 4,5-bisphosphate by SHIP2 controls glioblastoma cell migration through the organization of focal adhesions. PMID: 26826186
12. the dissociation process of the EphA2-SHIP2 SAM-SAM domain heterodimer complex the dissociation process of the EphA2-SHIP2 SAM-SAM domain heterodimer complex PMID: 26910424
13. Suppression of SHIP2 contributes to tumorigenesis and proliferation of gastric cancer cells via activation of Akt. PMID: 26201869
14. these findings suggest that SHIP2 is an important regulator of hepatic lipogenesis and lipoprotein secretion in insulin resistance state. PMID: 26456051
15. investigated the molecular link between SHIP2 expression and metabolic dyslipidemia using overexpression or suppression of SHIP2 gene in HepG2 cells PMID: 26188518
16. 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. PMID: 25383712
17. SHIP2 inhibition was accompanied by an increased Akt and FOXO-1 phosphorylation, whereas overexpression of the wild-type SHIP2 gene had the opposite effects PMID: 26123392
18. In conclusion, SHIP2 plays a key role in breast cancer stem cells of ER-negative breast cancers PMID: 24802135
19. 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. PMID: 25525286
20. 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 PMID: 25635986
21. The crystal structures of human SHIP2 in complex with phosphoinositide substrate analogs revealed a membrane interaction patch likely to assist in sequestering substrates from the lipid bilayer. PMID: 24704254
22. Association with SHIP2 and aging might depend on its effect on the insulin/IGF-1 pathway. PMID: 24313349
23. SHIP2 localization in intact cells is dependent on phosphorylation mechanisms on both Ser/Thr and Tyr residues. PMID: 24561238
24. Together, our result was shown that miR-184 might play a part in proliferation of HCC cells by INPPL1 loss and act as antiapoptotic factor in the development of HCC by inhibiting the activities of caspases 3/7. PMID: 24183204
25. SHIP2 play roles in normal development and at in cell proliferation in some cancer derived cells. [review] PMID: 24091101
26. SHIP2 expression is correlated with significant characteristics of hepatocellular carcinoma, and it may be useful as an unfavorable prognostic factor in HCC. PMID: 24228114
27. The results of this research suggested that SHIP2 expression was correlated with malignant phenotypes of non-small cell lung cancer and may thus serve as a poor prognostic factor and valuable oncogene for NSCLC. PMID: 24133597
28. INPPL1 is the disease gene for opsismodysplasia; opsismodysplasia has genetic heterogeneity. PMID: 23552673
29. mutations in inositol polyphosphate phosphatase-like 1 (INPPL1) cause opsismodysplasia with or without renal phosphate wasting. PMID: 23273567
30. INPPL1 mutations in OPS, a severe spondylodysplastic dysplasia with major growth plate disorganization, supports a key and specific role of this enzyme in endochondral ossification. PMID: 23273569
31. RhoA associates with SHIP2 to regulate cell polarization and migration. PMID: 22593208
32. Nephrin ligation resulted in abnormal morphology of actin tails in human podocytes when Ship2, Filamin or Lamellipodin were individually knocked down. PMID: 22194892
33. SHIP2 suppresses ligand-induced activation of EphA2 and promotes receptor coordinated chemotactic cell migration. PMID: 22244754
34. Caveolin-1 knockdown by small interfering RNA reduces H2O2-induced SHP-2 phosphorylation in rat primary astrocytes and in CRT-MG human astroglioma cells. PMID: 21918362
35. results support the hypothesis that SHIP2 may play a critical role in the initiation and progression of LSCC and may serve as both a prognostic marker and a potential therapeutic target in patients with LSCC PMID: 22079859
36. 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. PMID: 21770892
37. The upregulation of SHIP2 in Zucker rat glomeruli prior to the age of onset of proteinuria suggests a possible role for SHIP2 in the development of podocyte injury. PMID: 20654688
38. Treatment of HEKs and HCEKs with antago-205 increased SHIP2 levels and impaired the ability of these cells to seal linear scratch wounds compared with untreated or irrelevant-antago treatments PMID: 20530248
39. Data show that SHIP2 localizes to the nucleus and periphery, and has been shown to translocate to the cell membrane following EGF treatment. PMID: 19895833
40. LL5beta directs the translocation of filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2. PMID: 20236936
41. A recent study now shows that two additional tyrosines within Tir recruit the inositol phosphatase SHIP2 to generate a PI(3,4)P2-enriched membrane platform that stabilizes pedestal assembly. PMID: 20114020
42. The authors demonstrate that Y483 and Y511 within tandem ITIM-like sequences of Escherichia coli Tir are essential for recruiting human SHIP2, a host inositol phosphatase. PMID: 20114025
43. data highlight a novel biological role of the PP2A(T130) holoenzyme in EGF signaling through interaction with EGFR and the phosphatidylinositol (3,4,5)-trisphosphate 5-phosphatase SHIP2. PMID: 19825976
44. candidate gene for type 2 diabetes PMID: 12086927
45. overexpression strongly reduces the proliferation rate of K562 erythroleukemia cell line PMID: 12147234
46. SHIP phosphorylation by the immunoreceptor tyrosine-based activation motif (ITAM)-associated Fc gamma RIIa requires Shc phosphorylation, leads to activation of Src kinases, and down-regulates NF-kappa B-induced gene transcription during phagocytosis. PMID: 12370370
47. regulation of FcgammaR-mediated activation of human myeloid cells by the expression and function of the inositol phosphatase SHIP-2 PMID: 12690104
48. INPPL1 variants may impact susceptibility to disease and/or to subphenotypes involved in the metabolic syndrome in some diabetic patients. PMID: 15220217
49. Schizosaccharomyces pombe synaptojanin (SPsynaptojanin) and human SH2 domain-containing inositol-5-phosphatase SHIP2 comparison: substrate specificity and mechanism study PMID: 15316017
50. A novel regulatory role is suggested for SHIP2 in macrophage colony-stimulating factor (M-CSF)-stimulated myeloid cells. PMID: 15557176

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HGNC: 6080

OMIM: 125853

KEGG: hsa:3636

STRING: 9606.ENSP00000298229

UniGene: Hs.523875