anti-Adenosylhomocysteinase-Like 1 (AHCYL1) Anticorps

Human Adenosylhomocysteinase-Like 1 (AHCYL1) interaction partners

1. We investigated previously assumed interaction with AHCY-like-1 protein (AHCYL1), a paralog of AHCY. Indeed, significant interaction between both proteins exists. Additionally, silencing AHCYL1 leads to moderate inhibition of nuclear export of endogenous AHCY.

2. We have validated the vectors and confirmed self-association of AHCY, AHCYL1, and galectin-3. In a high-throughput BiFC screen, we identified new AHCY interaction partners: galectin-3 and PUS7L. We also describe additional steps in protein interaction analysis, applied for AHCY-galectin-3 interaction

3. These results suggest that by inhibiting Bcl2l10 activity and promoting contact between endoplasmic reticulum and mitochondria, IRBIT facilitates massive Ca(2+) transfer to mitochondria and promotes apoptosis.

4. IRBIT forms signaling complexes with PIPKIalpha and NBCe1-B, whose activity is regulated by PI(4,5)P2.

5. Formation of the Ribonucleotide reductase-IRBIT complex is regulated through phosphorylation of IRBIT, and ablation of IRBIT expression in HeLa cells causes imbalanced dNTP pools and altered cell cycle progression.

6. IRBIT is a master regulator of ion channels and ion transporters. (Review)

7. IRBIT plays an important role in intracellular pH regulation, mediated by NHE3, and further regulated by SPAK.

8. relationships between the WNK/SPAK and IRBIT/PP1 sites in the regulation of Na+-HCO3- cotransporters

9. conclude that AHCYL1 expression is associated with ovarian carcinogenesis as an oncogene in chickens, whereas it plays the role of tumor suppressor in human EOC, suggesting a paradoxical function of AHCYL1 in ovarian carcinogenesis

10. A NBCe1-B construct that lacks amino acid residues 2-16 of the amino-terminus is fully autoinhibited, but cannot be stimulated by IRBIT, indicating that autoinhibitory and IRBIT-binding determinants within the cytosolic amino-terminus are not identical.

11. Both IRBIT (inositol 1,4,5-trisphosphate receptor-binding protein) and WNK [with no lysine (K)] kinase have been implicated as additional HCO(3)(-) secretory controllers.

12. IRBIT opposes the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, in addition to stimulating their activities

13. IRBIT is critically involved in mediating activation of NHE3 by ANG II via a Ca(2+)/calmodulin-dependent protein kinases II-dependent pathway.

14. regulation through IRBIT enables NBC1 variants to have different physiological roles

15. An IRBIT homologue, Long-IRBIT, demonstrates only weak binding ability to inositol 1,4,5-trisphosphate receptor because of an inhibitory effect of its LISN domain, a Long-IRBIT specific N-terminal appendage.

Zebrafish Adenosylhomocysteinase-Like 1 (AHCYL1) interaction partners

1. AHCYL1 has a different function from AHCY and plays an important role in embryogenesis by modulating inositol 1,4,5-trisphosphate receptor function for the intracellular calcium release

Mouse (Murine) Adenosylhomocysteinase-Like 1 (AHCYL1) interaction partners

1. NHERF1 mediates ANG II-induced activation of renal NHE3, which requires coordination between IRBIT and the NHERF1 PDZ1 domain in binding and transporting NHE3

2. IRBIT forms signaling complexes with PIPKIalpha and NBCe1-B, whose activity is regulated by PI(4,5)P2.

3. IRBIT suppresses CaMKIIalpha activity and contributes to catecholamine homeostasis through TH phosphorylation.

4. Irbit was sequestered by InsP3 receptors (IP3Rs) in the endoplasmic reticulum

5. IRBIT opposes the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, in addition to stimulating their activities

6. IRBIT can directly interact with the IP3R, and that both the suppressor domain and the IP3-binding core of the IP3R are essential for a strong interaction.

7. phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R by IRBIT

8. Cloning, bacterial expression, and unique structure of adenosylhomocysteine hydrolase-like protein 1, or inositol 1,4,5-triphosphate receptor-binding protein.

9. Data show that pNBC1 activation requires the IRBIT PEST domain, while CFTR activation requires multiple domains, and suggest that IRBIT is a key coordinator of epithelial fluid and HCO3- secretion.

10. Results sugest that IRBIT modulates the polyadenylation state of specific mRNAs, both by controlling the cytoplasmic/nuclear partitioning of Fip1 and by inhibiting PAP activity, in response to a stimulus that alters its phosphorylation state.