AMPA, not NMDA, activates RhoA GTPases and subsequetly phosphorylates moesin

Kim, Sujin; Jeon, Songhee; Shin, Eun‐Young; Kim, Eung‐Gook; Park, Joobae; Bae, Chong Woo

doi:10.1038/emm.2004.14

Cited by 17 publications

(12 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previously, we reported that RhoA is involved in the phosphorylation of moesin in H19 -7/IGF-IR cells by glutamate (9,23). In the present study, we found that KCl induced the activation of Rac1, but not of RhoA, and that both RhoA and Rac1 are involved in the phosphorylation of ERM family proteins in neuronal cells, but importantly, that these two Rho family proteins are activated by different signaling pathways.…”

Section: Kcl-induced Rac1 Activation and Moesin Phosphorylation Are Dsupporting

confidence: 54%

“…It is well known that KCl induces depolarization of the plasma membrane and Ca 2ϩ influx into PC12 cells and subsequently activates diverse calcium-dependent signaling pathways, such as Ras-ERK. However, KCl-induced moesin phosphorylation was independent of the depolarization of the plasma membrane and Ca H19 -7/IGF-IR cells and that this process is independent of calcium influx (23). These results indicate that moesin in neuronal cells is phosphorylated by calcium-independent signaling pathways.…”

Section: Kcl-induced Rac1 Activation and Moesin Phosphorylation Are Dmentioning

confidence: 51%

See 1 more Smart Citation

Chloride Conductance Is Required for the Protein Kinase A and Rac1-dependent Phosphorylation of Moesin at Thr-558 by KCl in PC12 Cells

Jeon

Kim

et al. 2005

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Moesin is a member of the ERM family, a family of cross-linkers between the plasma membrane and the actin cytoskeleton, which are known to be activated by phosphorylation. Previously, we reported the RhoA and Rho kinase-dependent phosphorylation of moesin at Thr-558 in hippocampal neuronal cells by glutamate. Here we studied the induction of moesin phosphorylation by KCl (60 mM) in PC12 cells. Moesin phosphorylation at Thr-558 was increased after 2 min of KCl treatment, peaked at 5 min, and returned to the basal level by 60 min. KCl also activated Rac1, but not RhoA, in PC12 cells, and KCl-induced moesin phosphorylation was suppressed in dominant negative Rac1 (N17 Rac1)-expressed cells. The inhibition of protein kinase A (PKA), known as an upstream kinase of Rac1, abolished Rac1 activation and moesin phosphorylation by KCl. Interestingly, the phosphorylation of moesin by KCl was independent of KCl-induced membrane depolarization and calcium influx but was dependent on KCl-induced chloride conductance. 60 mM KCl induced chloride conductance in PC12 cells, and pretreatment with Cl ؊ channel blocker abolished Rac1 activation and moesin phosphorylation by KCl. These results suggest that the phosphorylation of moesin at Thr-558 in PC12 cells by KCl treatment is PKA-and Rac1-dependent and that KCl-induced chloride conductance is involved in the activation of this signaling system.

show abstract

Section: Kcl-induced Rac1 Activation and Moesin Phosphorylation Are Dsupporting

confidence: 54%

Section: Kcl-induced Rac1 Activation and Moesin Phosphorylation Are Dmentioning

confidence: 51%

Chloride Conductance Is Required for the Protein Kinase A and Rac1-dependent Phosphorylation of Moesin at Thr-558 by KCl in PC12 Cells

Jeon

Kim

et al. 2005

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…Activation of the AMPAR channel not only causes ion influx but also activates intracellular signaling pathways (Wang and Durkin, 1995;Wang et al, 1997;Hayashi et al, 1999;Kim et al, 2004). Furthermore, a recent study demonstrated the functional interaction between drebrin and Ras in spine plasticity (Biou et al, 2008).…”

Section: Involvement Of Ampar Activity In Spine Morphogenesismentioning

confidence: 99%

Activity of the AMPA receptor regulates drebrin stabilization in dendritic spine morphogenesis

Takahashi

Yamazaki

Hanamura

et al. 2009

Journal of Cell Science

View full text Add to dashboard Cite

Spine morphogenesis mainly occurs during development as a morphological shift from filopodia-like thin protrusions to bulbous ones. We have previously reported that synaptic clustering of the actin-binding protein drebrin in dendritic filopodia governs spine morphogenesis and synaptic PSD-95 clustering. Here, we report the activity-dependent cellular mechanisms for spine morphogenesis, in which the activity of AMPA receptors (AMPARs) regulates drebrin clustering in spines by promoting drebrin stabilization. In cultured developing hippocampal neurons, pharmacological blockade of AMPARs, but not of other glutamate receptors, suppressed postsynaptic drebrin clustering without affecting presynaptic clustering of synapsin I (synapsin-1). Conversely, the enhancement of the action of AMPARs promoted drebrin clustering in spines. When we explored drebrin dynamics by photobleaching individual spines, we found that AMPAR activity increased the fraction of stable drebrin without affecting the time constant of drebrin turnover. An increase in the fraction of stable drebrin corresponded with increased drebrin clustering. AMPAR blockade also suppressed normal morphological maturation of spines and synaptic PSD-95 clustering in spines. Together, these data suggest that AMPAR-mediated stabilization of drebrin in spines is an activity-dependent cellular mechanism for spine morphogenesis.

show abstract

“…Furthermore, the excitatory glutamate activates ROCK in neuronal cells (Jeon et al, 2002) and fasudil, a ROCK inhibitor, has been found to be neuroprotective against glutamate-related excitotoxicity (Kitaoka et al, 2004). Therefore, we speculated that there might be a link between these mechanisms and Rho-kinase pathway in depression, and it is possible that Y-27632 could block glutamatergic receptors-induced moesin phosphorylation (Kim et al, 2004) which may contribute to an antidepressant-like activity in rats.…”

Section: Discussionmentioning

confidence: 96%

Infralimbic cortex Rho-kinase inhibition causes antidepressant-like activity in rats

İnan

Soner

Şahin

2015

Progress in Neuro-Psychopharmacology and Biological Psychiatry

View full text Add to dashboard Cite

AMPA, not NMDA, activates RhoA GTPases and subsequetly phosphorylates moesin

Cited by 17 publications

References 17 publications

Chloride Conductance Is Required for the Protein Kinase A and Rac1-dependent Phosphorylation of Moesin at Thr-558 by KCl in PC12 Cells

Chloride Conductance Is Required for the Protein Kinase A and Rac1-dependent Phosphorylation of Moesin at Thr-558 by KCl in PC12 Cells

Activity of the AMPA receptor regulates drebrin stabilization in dendritic spine morphogenesis

Infralimbic cortex Rho-kinase inhibition causes antidepressant-like activity in rats

Contact Info

Product

Resources

About