CSF1R dimerizes

Stable Identifier
R-HSA-9680349
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
CSF1R dimerizes
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
After the CSF1 dimer or IL34 dimer binds a CSF1R monomer, a second molecule of CSF1R binds CSF1 and the two molecules of CSF1R dimerize by interaction of their D4 and D5 domains, resulting in a conformational change in CSF1R that activates its kinase activity (Elegheert et al. 2011, Felix et al. 2015, and inferred from mouse homologs). Disulfide bonds between the CSF1R monomers appear to be artifacts of immunoprecipitation, reflecting a conformational change following CSF1R dimerization (inferred from mouse homologs).
Literature References
PubMed ID Title Journal Year
22153499 Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles

Elegheert, J, Desfosses, A, Shkumatov, AV, Wu, X, Bracke, N, Verstraete, K, Van Craenenbroeck, K, Brooks, BR, Svergun, DI, Vergauwen, B, Gutsche, I, Savvides, SN

Structure 2011
26235028 Structure and Assembly Mechanism of the Signaling Complex Mediated by Human CSF-1

Felix, J, De Munck, S, Verstraete, K, Meuris, L, Callewaert, N, Elegheert, J, Savvides, SN

Structure 2015
Participants
Input
Output
Participates
as an event of
Inferred From
Csf1r dimerizes (Mus musculus)
Authored
May, B  (2020-03-14)
Reviewed
Stanley, ER  (2022-10-06)
Created
May, B  (2020-03-27)
Cite Us!