Drosophila OTK Is a Glycosaminoglycan-Binding Protein with High Conformational Flexibility

Daniel Rozbesky*, Jim Monistrol, Vitul Jain, James Hillier, Sergi Padilla-Parra, E. Yvonne Jones

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

The transmembrane protein OTK plays an essential role in plexin and Wnt signaling during Drosophila development. We have determined a crystal structure of the last three domains of the OTK ectodomain and found that OTK shows high conformational flexibility resulting from mobility at the interdomain interfaces. We failed to detect direct binding between Drosophila Plexin A (PlexA) and OTK, which was suggested previously. We found that, instead of PlexA, OTK directly binds semaphorin 1a. Our binding analyses further revealed that glycosaminoglycans, heparin and heparan sulfate, are ligands for OTK and thus may play a role in the Sema1a-PlexA axon guidance system.

Original languageEnglish
Pages (from-to)507-515.e5
JournalStructure
Volume28
Issue number5
DOIs
Publication statusPublished - 5 May 2020

Keywords

  • GAG
  • glycosaminoglycans
  • Ig-like domain
  • Off-track
  • OTK
  • PlexA
  • plexin
  • Sema1a
  • signaling
  • Wnt

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