Dimerization of Tie2/Ang1 complex

Stable Identifier
R-HSA-210881
Type
Reaction [binding]
Species
Homo sapiens
Compartment
plasma membrane
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
Dimerization of Tie2/Ang1 complex
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Receptor tyrosine kinase activation and signaling are typically initiated via dimerization of the receptors through homo-oligomeric ligand binding.

Angiopoietin1 may form homotrimers, but in most cases it assembles into higher-order multimers. This oligomerization is mediated by the N-ter coiled coil domain (CCD).
The binding of Ang1 oligomers to Tie2 promotes the dimerization of Tie2, which is further assisted by the interaction between the kinase domains of the receptors.
Literature References
PubMed ID Title Journal Year
14749497 Functional significance of Tie2 signaling in the adult vasculature

Peters, KG, Wong, AL, Sankar, S, Huang, L, Kontos, CD, Dewhirst, MW, Rao, P, Lin, PC

Recent Prog Horm Res 2004
Participants
Input
Output
Participates
as an event of
Orthologous Events
Dimerization of Tie2/Ang1 complex (Bos taurus)
Dimerization of Tie2/Ang1 complex (Canis familiaris)
Dimerization of Tie2/Ang1 complex (Danio rerio)
Dimerization of Tie2/Ang1 complex (Gallus gallus)
Dimerization of Tie2/Ang1 complex (Mus musculus)
Dimerization of Tie2/Ang1 complex (Rattus norvegicus)
Dimerization of Tie2/Ang1 complex (Sus scrofa)
Dimerization of Tie2/Ang1 complex (Xenopus tropicalis)
Authored
Garapati, P V  (2008-03-05)
de Bono, B  (2008-03-05)
Reviewed
Trowsdale, J  (2008-02-26)
Created
Garapati, P V  (2008-01-17)
Cite Us!