anti-Adaptor Protein, phosphotyrosine Interaction, PH Domain and Leucine Zipper Containing 1 (APPL1) Antikörper

Human Adaptor Protein, phosphotyrosine Interaction, PH Domain and Leucine Zipper Containing 1 (APPL1) Interaktionspartner

1. Present study demonstrated that expression of APPL1 protein and mRNA was upregulated in gastric carcinoma (GC) tissues and cell lines. The expression of APPL1 in GC was statistically associated with metastasis stage. Overexpression of APPL1 promotes invasion and metastasis of gastric cancer cells and the underlying molecular mechanism may facilitate EMT via Akt2 phosphorylation.

2. APPL1 positively mediated leptin signaling.

3. Decreased expression of APPL1 is associated with polycystic ovary syndrome.

4. Results indicate that persistent rab5 overactivation through beta-cleaved carboxy-terminal fragment of APP-APPL1 interactions constitutes a novel APP-dependent pathogenic pathway in Alzheimer's disease

5. Data show that signal transducing adaptor proteins APPL1 and APPL2 are required for TGFbeta-induced nuclear translocation of TGFbeta type I receptor (TbetaRI)-ICD and for cancer cell invasiveness of prostate and breast cancer cell lines.

6. Low expression of APPL1 is associated with metastasis in prostate cancer.

7. APPL1 endosomes represent a distinct population of Rab5-positive sorting endosomes.

8. article provides evidence that GG genotype and G carrier (CG+GG) genotypes of the rs4640525 polymorphism in the APPL1 gene may be suitable susceptibility biomarkers for NAFLD

9. Two loss-of-function mutations in APPL1, identified by means of whole-exome sequencing, found in two large families with a high prevalence of Familial Diabetes Mellitus.

10. A role for APPL1 in TLR3/4-dependent TBK1 and IKKepsilon activation in macrophages.

11. ATM is the central modulator of APPL-mediated effects on radiosensitivity and DNA repair.

12. APPL1 sensitizes insulin signaling by acting at a site downstream of the IR. Study uncovers a mechanism regulating insulin signaling and crosstalk between the insulin and adiponectin pathways.

13. APPL1 is a positive regulator of Dvl2-dependent transcriptional activity of AP-1.

14. It concludes that APPL1(PH) binding to BAR domain and Reptin is mutually exclusive which regulates the nucleocytoplasmic shuttling of Reptin.

15. The activated EGF receptor enters distinct sub-populations of SNX15- and APPL1-labelled peripheral endocytic vesicles.

16. C-APPL1/A-APPL2 allele combination is associated with non-alcoholic fatty liver disease occurrence, with a more severe hepatic steatosis grade and with a reduced adiponectin cytoprotective effect on liver.

17. TRAF6-mediated ubiquitination of APPL1 is a vital step for the hepatic actions of insulin through modulation of membrane trafficking and activity of Akt.

18. Rab5a and APPL1 are overexpressed in breast cancer, and are positively correlated with the HER-2 expression.

19. neurons with APPL1-positive granules were restricted to the CA1 area and subiculum, areas associated with hippocampal vulnerability, suggesting a possible link between the perisomatic accumulation of APPL1 and Alzheimer's disease.

20. APPL1 regulates basal NF-kappaB activity by modulating the stability of NIK, which affects the activation of p65.

Mouse (Murine) Adaptor Protein, phosphotyrosine Interaction, PH Domain and Leucine Zipper Containing 1 (APPL1) Interaktionspartner

1. APPL1 enhances glucose uptake by modulating the activation and localization of PKCzeta, as well as its functional interaction with both PP2A and myosin IIa.

2. APPL1-SirT1-STAT3 pathway mediated adiponectin signaling in primary hepatocytes.

3. Here we establish potential roles for APPL1 and 2 signaling adaptors as regulators of LPS/TLR4-induced signaling, transcription, and cytokine secretion.

4. Appl1/2-null mouse embryonic fibroblasts exhibited defects in HGF-induced Akt activation, migration, and invasion.

5. In experimental high glucose condition APPL1 acts as a protective factor against podocytes injury through regulating AMPK signaling.

6. A role for APPL1 in TLR3/4-dependent TBK1 and IKKepsilon activation in macrophages.

7. APPL1 sensitizes insulin signaling by acting at a site downstream of the IR. Study uncovers a mechanism regulating insulin signaling and crosstalk between the insulin and adiponectin pathways.

8. Study demonstrates the roles of APPL1 in regulating GSIS and mitochondrial function in pancreatic beta cells, which implicates APPL1 as a therapeutic target in the treatment of type 2 diabetes.

9. APPL1 transgenic mice exhibit improved peripheral metabolism, reduced cardiac lipotoxicity, and improved insulin sensitivity.

10. Our findings demonstrate that exercise training performed concomitantly to a high-fat diet reduces the degree of insulin resistance and improves adipoR1-2/APPL1 protein levels in the hepatic, adipose, and skeletal muscle tissue

11. APPL1 contributes to connecting synaptic NMDA receptors with the intracellular phosphoinositide 3-kinase /Akt cascade in neurons.

12. Reduced APPL1 expression in pancreatic islets may serve as a pathological link that couples insulin resistance to beta-cell dysfunction in type 2 diabetes.

13. Endurance training was able to increase APPL1 expression.

14. APPL1 plays a key role in coordinating the vasodilator and vasoconstrictor effects of insulin by modulating Akt-dependent NO production and ERK1/2-mediated ET-1 secretion in the endothelium.

15. Data found that the inhibitory effect of adiponectin on osteoclasts was induced by APPL1-mediated down-regulation of Akt1 activity.

16. Appl1 is dispensable for Akt signaling in vivo and T-cell differentiation.

17. The promyogenic function of Cdo involves a coordinated activation of p38MAPK and Akt via association with scaffold proteins, JLP and Bnip-2 for p38MAPK and APPL1 for Akt.

18. Appl proteins are required for HGF-induced cell survival and migration via activation of Akt

19. APPL1 interacts with adiponectin receptors in mammalian cells and the interaction is stimulated by adiponectin.

20. Overexpression of APPL1 protein in the liver of db/db obese mice suppressed the interaction between Proto-Oncogene Proteins c-akt and TRB3 protein.