Reactome | Limk1 phosphorylates Cfl1, inactivating it

Limk1 phosphorylates Cfl1, inactivating it

Stable Identifier

R-NUL-421139

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, extracellular region, plasma membrane

ReviewStatus

5/5

General

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SVG | | PPTX | SBGN

Limk1 phosphorylates Cfl1, inactivating it

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).

Literature References

PubMed ID	Title	Journal	Year
12642619	Regulation of growth cone actin dynamics by ADF/cofilin Bamburg, JR, Gungabissoon, RA	J Histochem Cytochem	2003
11276226	Phosphorylation of cofilin by LIM-kinase is necessary for semaphorin 3A-induced growth cone collapse Sekine-Aizawa, Y, Wakatsuki, S, Sehara-Fujisawa, A, Ohashi, K, Goshima, Y, Aizawa, H, Moriyama, K, Yahara, I, Ishii, A, Mizuno, K, Sasaki, Y	Nat Neurosci	2001