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Details on Person The EPHB2-FAK pathway partially promotes dendritic spine sta...
| Class:Id | Summation:3928315 |
|---|---|
| _displayName | The EPHB2-FAK pathway partially promotes dendritic spine sta... |
| _timestamp | 2013-10-03 09:45:45 |
| created | [InstanceEdit:3928288] Garapati, P V, 2013-07-22 |
| literatureReference | [LiteratureReference:3928042] Focal adhesion kinase acts downstream of EphB receptors to maintain mature dendritic spines by regulating cofilin activity [LiteratureReference:399912] Regulation of growth cone actin dynamics by ADF/cofilin |
| modified | [InstanceEdit:4420372] Garapati, P V, 2013-09-03 [InstanceEdit:4640880] Garapati, P V, 2013-09-27 [InstanceEdit:4655451] Garapati, P V, 2013-10-03 [InstanceEdit:4655453] Garapati, P V, 2013-10-03 |
| text | The EPHB2-FAK pathway partially promotes dendritic spine stability through LIMK-mediated cofilin (CFL1) phosphorylation (Shi et al. 2009). CFL1 is a member of the ADF (actin-depolymerizing factor) protein family that is involved in regulating actin dynamics in the growth cone. It binds to actin in a one-to-one molar ratio, and stimulates both the severing of actin filaments and depolymerization of actin subunits from the actin filament end. Activated LIMK phosphorylates CFL1 on the conserved serine 3 residue located near the actin-binding site. After phosphorylation, CFL1 is inactive, loses its affinity for actin and dissociates from G-actin monomers. Once freed, ADP-actin monomers can exchange ADP with cytoplasmic ATP, ready for reincorporation at the barbed end of a growing filament (Gungabissoon & Bamburg 2003). |
| (summation) | [Reaction:3928608] LIMK phosphorylates CFL1, inactivating it [Homo sapiens] |
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