RAS (RAD and GEM)-Like GTP Binding 2 Proteins (REM2)

Mouse (Murine) RAS (RAD and GEM)-Like GTP Binding 2 (REM2) interaction partners

1. Rem2 stabilizes intrinsic excitability and spontaneous firing in visual circuits.

2. report that substitution of two key amino acid residues in the Rem2 N terminus (Arg-79 and Arg-80) completely abolishes its ability to inhibit CaMKII

3. Our results highlight Rem2 as a unique molecule that transduces changes in neuronal activity detected at the cell membrane to morphologically relevant changes in gene expression in the nucleus

4. Study have shown that Rem2 is expressed in a variety of nervous system tissues, but is enriched in the basal ganglia. The function of Rem2 in the basal ganglia is unknown, but may be important for neuronal maturation during development, and/or neuroplasticity in adulthood.

5. Nuclear localization of RGK proteins (Rad, Rem, and Rem2) contributes to the suppression of RGK-mediated cell shape remodeling.

6. Voltage dependant calcium channels blockade by Rem2 is likely to be controlled by both the localized concentration of membrane phosphorylated phosphatidylinositide lipids and direct 14-3-3 binding to the Rem2 C-terminus.

Human RAS (RAD and GEM)-Like GTP Binding 2 (REM2) interaction partners

1. 2 novel gene variants in REM2 and KCNK17 that provide a physiologically plausible explanation for variable expressivity in a large subset of patients in a multigenerational long QT syndrome type 2 family

2. report that substitution of two key amino acid residues in the Rem2 N terminus (Arg-79 and Arg-80) completely abolishes its ability to inhibit CaMKII

3. conclude that endogenous Rem2 is a positive regulator of functional, excitatory synapse development and a negative regulator of dendritic complexity

4. Rem2 has a role in neuronal plasticity hrough co-trafficking with CaMKIIa

5. molecular mechanisms by which Rem2 knockdown affected synaptogenesis and Ca(2) homeostasis in cultured rat hippocampal neurons

6. our results suggest that Rem2 regulates dendritic branching and synapse development

7. Rem2 mediates the fibroblastic growth factor 2 (FGF2) signaling pathway to maintain proliferation of hESCsby suppressing the transcriptional activity of p53 and cyclin D(1)

8. inhibition of L-type Ca2+ channels by Rem2 signaling may represent a new and potentially important mechanism for regulating Ca2+-triggered exocytosis in hormone-secreting cells, including insulin secretion in pancreatic beta-cells

9. data unravel a possible molecular mechanism for Rem2-induced angiogenesis and suggests Rem2 as a potential novel target for treating pathological angiogenesis