Activation of LIMK1 by binding to the BMP receptor, BMPRII, regulates BMP-dependent dendritogenesis
AUTOR(ES)
Lee-Hoeflich, Si Tuen
FONTE
Nature Publishing Group
RESUMO
The growth and morphological differentiation of dendrites are critical events in the establishment of proper neuronal connectivity and neural function. One extrinsic factor, BMP7, has been shown to specifically affect dendritic morphogenesis; however, the underlying mechanism by which this occurs is unknown. Here we show that LIM kinase 1 (LIMK1), a key downstream effector of Rho GTPases, colocalizes with the BMP receptor, BMPRII, in the tips of neurites and binds to BMPRII. This interaction is required for BMP-dependent induction of the dendritic arbor in cortical neurons. Furthermore, we demonstrate that the physical interaction of LIMK1 with BMPRII synergizes with the Rho GTPase, Cdc42, to activate LIMK1 catalytic activity. These studies thus define a Smad-independent pathway that directly links the BMP receptor to regulation of actin dynamics and provides insights into how extracellular signals modulate LIMK1 activity to permit fine spatial control over cytoskeletal remodelling during dendritogenesis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=535083Documentos Relacionados
- Regulation of actin function by protein kinase A-mediated phosphorylation of Limk1
- LIMK1 Regulates Golgi Dynamics, Traffic of Golgi-derived Vesicles, and Process Extension in Primary Cultured NeuronsD⃞
- BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II
- Complex effects of rexinoids on ligand dependent activation or inhibition of the xenobiotic receptor, CAR
- Activation of latent myostatin by the BMP-1/tolloid family of metalloproteinases