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When unphosphorylated, dematin's two F-actin binding domains move independent of one another permitting them to bind different F-actin filaments.
the headpiece domain of dematin (show EPB49 Antibodies) regulates calcium mobilization and signaling in platelets
a novel functional role for dematin (show EPB49 Antibodies) in regulating erythrocyte membrane function.
Fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin (show EPB49 Antibodies) headpiece C-terminal. The reduction of mobility in the loop region upon the S74E mutation can be seen from the (15)N order parameters.
results suggest that phosphorylation of the dematin (show EPB49 Antibodies) headpiece acts as a conformational switch within this headpiece domain
a crucial role for this proline residue in structural stability and folding potential of HP (sub)domains consistent with Pro-Trp (show TBPL1 Antibodies) stacking as a more general determinant of protein stability
study investigated motions in the backbone of dematin (show EPB49 Antibodies) headpiece domain and its mutant DHPS74E using several complementary NMR relaxation techniques
results suggest that the core domain of dematin (show EPB49 Antibodies) exhibits properties typical of a natively unfolded protein, while the headpiece domain is folded in a conformation essentially identical to its native structure
Dematin, or EPB49, is an actin-bundling protein originally identified in the erythroid membrane skeleton. Its actin-bundling activity is abolished upon phosphorylation by cAMP-dependent protein kinase and is restored after dephosphorylation (Rana et al., 1993
, dematin actin-binding protein
, erythrocyte membrane protein band 4.9 (dematin)