RhoA is activated by nucleotide exchange and inhibits axonal growth

Stable Identifier
R-HSA-194518
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane
ReviewStatus
5/5
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RhoA is activated by nucleotide exchange and inhibits axonal growth
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RHOA is activated by guanine nucleotide exchange factors (RhoGEFs), exchanging GDP for GTP. RHOA, activated following binding of MDGIs (RTN4, MAG or OMG) to the complex of NOGO receptor (RTN4R, also known as NgR) and NGFR (p75NTR), rigidifies the actin cytoskeleton, thereby inhibiting axonal elongation and causing growth cone collapse. MCF2 (Dbl) RHO GEF was used to demonstrate activation of RHOA downstream of NGFR and RTN4R-mediated sequestration of ARHGDIA, a RHO-GDI, but other RHO GEFs may also be involved in RHOA activation (Yamashita and Tohyama 2003).

Literature References
PubMed ID Title Journal Year
12692556 The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI

Yamashita, T, Tohyama, M

Nat Neurosci 2003
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Output
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as an event of
Catalyst Activity

guanyl-nucleotide exchange factor activity of MCF2 [cytosol]

Physical Entity
MCF2 [cytosol] (Homo sapiens)
Activity
guanyl-nucleotide exchange factor activity (GO:0005085)
Orthologous Events
RhoA is activated by nucleotide exchange and inhibits axonal growth (Bos taurus)
RhoA is activated by nucleotide exchange and inhibits axonal growth (Canis familiaris)
RhoA is activated by nucleotide exchange and inhibits axonal growth (Danio rerio)
RhoA is activated by nucleotide exchange and inhibits axonal growth (Gallus gallus)
RhoA is activated by nucleotide exchange and inhibits axonal growth (Mus musculus)
RhoA is activated by nucleotide exchange and inhibits axonal growth (Rattus norvegicus)
RhoA is activated by nucleotide exchange and inhibits axonal growth (Sus scrofa)
RhoA is activated by nucleotide exchange and inhibits axonal growth (Xenopus tropicalis)
Authored
Nasi, S  (2006-10-10)
Annibali, D  (2006-10-10)
Reviewed
Friedman, WJ  (2008-05-20)
Chao, MV  (2008-05-28)
Created
Jassal, B  (2007-03-22)
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