Functional binding of E-selectin to its ligands is enhanced by structural features beyond its lectin domain.
E-selectin
adhesion
binding kinetics
carbohydrate-binding protein
cell adhesion
cell migration
complement regulatory repeats
conformational extension
dimerization
glycobiology
glycoprotein
glycoprotein structure
homing
kinetics
short consensus repeats
silkworm expression
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
13 03 2020
13 03 2020
Historique:
received:
19
09
2019
revised:
12
01
2020
pubmed:
18
1
2020
medline:
15
12
2020
entrez:
18
1
2020
Statut:
ppublish
Résumé
Selectins are key to mediating interactions involved in cellular adhesion and migration, underlying processes such as immune responses, metastasis, and transplantation. Selectins are composed of a lectin domain, an epidermal growth factor (EGF)-like domain, multiple short consensus repeats (SCRs), a transmembrane domain, and a cytoplasmic tail. It is well-established that the lectin and EGF domains are required to mediate interactions with ligands; however, the contributions of the other domains in mediating these interactions remain obscure. Using various E-selectin constructs produced in a newly developed silkworm-based expression system and several assays performed under both static and physiological flow conditions, including flow cytometry, glycan array analysis, surface plasmon resonance, and cell-rolling assays, we show here that a reduction in the number of SCR domains is correlated with a decline in functional E-selectin binding to hematopoietic cell E- and/or L-selectin ligand (HCELL) and P-selectin glycoprotein ligand-1 (PSGL-1). Moreover, the binding was significantly improved through E-selectin dimerization and by a substitution (A28H) that mimics an extended conformation of the lectin and EGF domains. Analyses of the association and dissociation rates indicated that the SCR domains, conformational extension, and dimerization collectively contribute to the association rate of E-selectin-ligand binding, whereas just the lectin and EGF domains contribute to the dissociation rate. These findings provide the first evidence of the critical role of the association rate in functional E-selectin-ligand interactions, and they highlight that the SCR domains have an important role that goes beyond the structural extension of the lectin and EGF domains.
Identifiants
pubmed: 31949047
pii: S0021-9258(17)48637-6
doi: 10.1074/jbc.RA119.010910
pmc: PMC7076219
pii:
doi:
Substances chimiques
E-Selectin
0
Immobilized Proteins
0
Ligands
0
Polysaccharides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3719-3733Informations de copyright
© 2020 Aleisa et al.
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