Browse our anti-erythrocyte Membrane Protein Band 4.9 (Dematin) (EPB49) Antibodies

Human erythrocyte Membrane Protein Band 4.9 (Dematin) (EPB49) interaction partners

1. When unphosphorylated, dematin's two F-actin binding domains move independent of one another permitting them to bind different F-actin filaments.

2. the headpiece domain of dematin regulates calcium mobilization and signaling in platelets

3. a novel functional role for dematin in regulating erythrocyte membrane function.

4. Fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin headpiece C-terminal. The reduction of mobility in the loop region upon the S74E mutation can be seen from the (15)N order parameters.

5. results suggest that phosphorylation of the dematin headpiece acts as a conformational switch within this headpiece domain

6. a crucial role for this proline residue in structural stability and folding potential of HP (sub)domains consistent with Pro-Trp stacking as a more general determinant of protein stability

7. study investigated motions in the backbone of dematin headpiece domain and its mutant DHPS74E using several complementary NMR relaxation techniques

8. results suggest that the core domain of dematin exhibits properties typical of a natively unfolded protein, while the headpiece domain is folded in a conformation essentially identical to its native structure

Mouse (Murine) erythrocyte Membrane Protein Band 4.9 (Dematin) (EPB49) interaction partners

1. results demonstrate that dematin plays a critical role in maintaining the fundamental properties of the membrane cytoskeleton complex.

2. the headpiece domain of dematin regulates calcium mobilization and signaling in platelets

3. remodeling of the host cell directed Plasmodium includes the recruitment of dematin, an actin-binding protein of the erythrocyte membrane skeleton and its repositioning to the parasite

4. physiological significance of dematin and demonstrate a role for the headpiece domain in the maintenance of structural integrity and mechanical properties of erythrocytes in vivo.

5. Dematin plays an essential role in the maintenance of erythrocyte shape and membrane stability; dematin-membrane interaction could link the junctional complex to the plasma membrane in erythroid cells.

6. Dematin is expressed in skin, mostly in dermal fibroblasts and hypodermal adipocytes. Knockout mice lacking dematin exhibit hair loss.

7. These results unveil a new function of dematin as a negative regulator of the RhoA activation pathway with physiological implications for normal and pathogenic signaling pathways.