Membrane-bound CDH11 is cleaved to produce secreted CDH11 isoform

Stable Identifier
R-HSA-9759522
Type
Reaction [uncertain]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
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
The canonical isoform of human CDH11, but not the variant isoform, is cleaved to produce an 80 kDa secreted fragment (Kawaguchi et al 1999). The exact cleavage site is not known but based on the size of the secreted fragment is predicted to occur close to the boundary of ectodomains EC3 and EC4. In Xenopus laevis, the orthologues cleavage, which occurs during the migration of cranial neural crest cells, can be performed by either ADAM13 or ADAM9 metalloproteinases, but not ADAM19 (McCusker et al. 2009). The cleavage of Xenopus cadherin-11 by ADAM13 appears to be biologically relevant (Abbruzzese et al. 2014). The closest human orthologues of Xenopus ADAM13 are ADAM19 and ADAM33, which are annotated as candidate metalloproteinases.
Literature References
PubMed ID Title Journal Year
10320525 Expression and function of the splice variant of the human cadherin-11 gene in subordination to intact cadherin-11

Machinami, R, Takeshita, S, Kawaguchi, J, Kashima, T, Imai, T, Kudo, A

J Bone Miner Res 1999
Participants
Participates
Catalyst Activity

metallopeptidase activity of (ADAM33,ADAM19)

Orthologous Events
Authored
Reviewed
Created
Cite Us!