PECAM-1 supports leukocyte diapedesis by tension-dependent dephosphorylation of VE-cadherin.
Actomyosin
/ metabolism
Animals
Antigens, CD
/ chemistry
Cadherins
/ chemistry
Calcium Signaling
Gene Knock-In Techniques
Human Umbilical Vein Endothelial Cells
Humans
Leukocytes
/ cytology
Mice
Phosphorylation
Platelet Endothelial Cell Adhesion Molecule-1
/ metabolism
Protein Tyrosine Phosphatase, Non-Receptor Type 11
/ metabolism
Transendothelial and Transepithelial Migration
Tyrosine
/ chemistry
VE-cadherin
cell adhesion
endothelial junctions
leukocyte extravasation
mechanical tension
Journal
The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664
Informations de publication
Date de publication:
03 05 2021
03 05 2021
Historique:
revised:
15
01
2021
received:
01
07
2020
accepted:
27
01
2021
pubmed:
20
2
2021
medline:
5
11
2021
entrez:
19
2
2021
Statut:
ppublish
Résumé
Leukocyte extravasation is an essential step during the immune response and requires the destabilization of endothelial junctions. We have shown previously that this process depends in vivo on the dephosphorylation of VE-cadherin-Y731. Here, we reveal the underlying mechanism. Leukocyte-induced stimulation of PECAM-1 triggers dissociation of the phosphatase SHP2 which then directly targets VE-cadherin-Y731. The binding site of PECAM-1 for SHP2 is needed for VE-cadherin dephosphorylation and subsequent endocytosis. Importantly, the contribution of PECAM-1 to leukocyte diapedesis in vitro and in vivo was strictly dependent on the presence of Y731 of VE-cadherin. In addition to SHP2, dephosphorylation of Y731 required Ca
Identifiants
pubmed: 33604918
doi: 10.15252/embj.2020106113
pmc: PMC8090850
doi:
Substances chimiques
Antigens, CD
0
Cadherins
0
Pecam1 protein, mouse
0
Platelet Endothelial Cell Adhesion Molecule-1
0
cadherin 5
0
Tyrosine
42HK56048U
Actomyosin
9013-26-7
Protein Tyrosine Phosphatase, Non-Receptor Type 11
EC 3.1.3.48
Ptpn11 protein, mouse
EC 3.1.3.48
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e106113Informations de copyright
© 2021 The Authors. Published under the terms of the CC BY NC ND 4.0 license.
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