N-glycosylation of ephrin B1 modulates its function and confers therapeutic potential in B-cell lymphoma.

ABSTRACT: Given the pivotal role of the Eph-Ephrin signaling pathway in tumor progression, agonists or antagonists targeting Eph-Ephrin have emerged as promising anticancer strategies. However, the implications of glycosylation modifications within Eph-Ephrin and their targeted protein therapeutics remain elusive. Here, we identify that N-glycosylation within the receptor-binding domain (RBD) of ephrin B1 (EFNB1) is indispensable for its functional repertoire. Notably, compared with wildtype EFNB1, the glycosylation-deficient N139D mutant drastically diminishes the sensitivity of tumor cells with chemotherapeutic agents, suggesting the existence of both glycosylation-dependent and -independent effects mediated by EFNB1. Transcriptomic analysis highlights immune response and oxidative phosphorylation

SUBMITTER: Li X 

PROVIDER: S-EPMC11871495 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature