Biological and structural characterization of glycosylation on ephrin-a1, a preferred ligand for EPHA2 receptor tyrosine kinase

Sara Ferluga, Roy Hantgan, Yehuda Goldgur, Juha P. Himanen, Dimitar B. Nikolov, Waldemar Debinski

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

Background: Ephrin-A1 is the preferred ligand for EphA2 receptor. Results: Biological assays and crystal structure analysis document that ephrin-A1 deglycosylation abrogates ligand's binding and receptor activation, and also protein folding and cellular localization. Conclusion: The glycosylation of ephrin-A1 enables EphA2 receptor binding and activation by stabilizing Eph/ephrin heterotetramers. Significance: The glycosylation of ephrin-A1 is indispensable for the protein biological activity.

Original languageEnglish
Pages (from-to)18448-18457
Number of pages10
JournalJournal of Biological Chemistry
Volume288
Issue number25
DOIs
StatePublished - 21 Jun 2013
Externally publishedYes

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