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

doi:10.1074/jbc.M113.464008

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 journal › Article › peer-review

25 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 language	English
Pages (from-to)	18448-18457
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	288
Issue number	25
DOIs	https://doi.org/10.1074/jbc.M113.464008
State	Published - 21 Jun 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.464008

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

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.",

author = "Sara Ferluga and Roy Hantgan and Yehuda Goldgur and Himanen, {Juha P.} and Nikolov, {Dimitar B.} and Waldemar Debinski",

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T1 - Biological and structural characterization of glycosylation on ephrin-a1, a preferred ligand for EPHA2 receptor tyrosine kinase

AU - Ferluga, Sara

AU - Hantgan, Roy

AU - Goldgur, Yehuda

AU - Himanen, Juha P.

AU - Nikolov, Dimitar B.

AU - Debinski, Waldemar

PY - 2013/6/21

Y1 - 2013/6/21

N2 - 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.

AB - 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.

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U2 - 10.1074/jbc.M113.464008

DO - 10.1074/jbc.M113.464008

M3 - Article

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VL - 288

SP - 18448

EP - 18457

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 25

ER -

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

Abstract

ASJC Scopus subject areas

UN SDGs

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