anti-Amyloid beta (A4) Precursor Protein-Binding, Family A, Member 3 (APBA3) Antibodies

Mouse (Murine) Amyloid beta (A4) Precursor Protein-Binding, Family A, Member 3 (APBA3) interaction partners

1. APBA3-deficient mice show reduced metastasis, with no apparent effect on primary tumor growth. APBA3 deficiency in inflammatory monocytes hampers glycolysis-dependent chemotaxis of cells toward metastatic sites.

2. we have identified Mint3 as a physiological positive regulator of TLR3/4 and RIG-I-induced IFN-beta production and have outlined a feedback mechanism for the control of antiviral immune responses.

3. Mint3 depletion attenuated metastasis to the lungs in breast cancer model mice.

4. Deletion of the Mint3/Apba3 gene in mice abrogates macrophage functions and increases resistance to lipopolysaccharide-induced septic shock.

5. Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV

6. Mints are important regulators of presynaptic neurotransmitter release that are essential for mouse survival.

7. Binding of Munc18-1 to closed, target-SNARE syntaxin 1 stimulates vesicle docking and regulates the consecutive priming step during exocytosis of secretory or synaptic vesicles.

8. X11L2 functions in the nucleus by a mechanism distinct from conventional transactivators

Human Amyloid beta (A4) Precursor Protein-Binding, Family A, Member 3 (APBA3) interaction partners

1. Results suggest that NECAB3, a novel Mint3-binding protein, activates HIF-1 to promote normoxic glycolysis and tumorigenicity by forming a ternary complex with Mint3 and FIH-1.

2. FIH-1-Mint3 axis does not control HIF-1 transcriptional activity in nucleus pulposus cells.

3. Mints are necessary for activity-induced APP and PS1 trafficking and provide insight into the cellular fate of APP in endocytic pathways essential for Abeta production.

4. Strict specificity for recruitment of the Mint3 adaptor by APP at the Golgi, a critical role for Tyr-682 (within the YENPTY motif) in Mint3 recruitment and export of APP from the Golgi, are demonstrated.

5. These results indicate that all three amyloid beta protein precursor family members are capable of activating gene transcription via Mint3-Taz and Mint3-Yap.

6. Two transcriptional coactivators, TAZ and YAP, functionally associate with amyloid precursor protein through Mint3 and form transcriptionally active triple protein complexes.

7. Associated with etilogical mechanism of Alzheimer's disease.

8. Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV

9. We have examined the ability of Bcr to interact with other epithelial PDZ proteins and found specific binding to both the apical PDZK1 protein and the Golgi-localized Mint3

10. These data implicate Mint3 activity as a critical determinant of post-Golgi APP traffic.

11. the interaction between the PTB domain of Mint3 and the acidic peptide signal of Furin regulates the specific localization of Furin in the trans-Golgi network

12. Mint3 regulates the FIH-1-HIF-1 pathway, which controls ATP production in macrophages