Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls

Melina Velasquez, Juan Salgado Salter, Javier Gloazzo Dorosz, Bent L. Petersen, José M. Estevez

Research output: Contribution to journalReview articlepeer-review

35 Citations (Scopus)

Abstract

The genetic set up and the enzymes that define the O-glycosylation sites and transfer the activated sugars to cell wall glycoprotein Extensins (EXTs) have remained unknown for a long time. We are now beginning to see the emerging components of the molecular machinery that assembles these complex O-glycoproteins on the plant cell wall. Genes conferring the posttranslational modifications, i.e., proline hydroxylation and subsequent O-glycosylation, of the EXTs have been recently identified. In this review we summarize the enzymes that define the O-glycosylation sites on the O-glycoproteins, i.e., the prolyl 4-hydroxylases (P4Hs), the glycosyltransferases that transfer arabinose units (named arabinosyltransferases, AraTs), and the one responsible for transferring a single galactose (galactosyltransferase, GalT) on the protein EXT backbones. We discuss the effects of posttranslational modifications on the structure and function of extensins in plant cell walls.

Original languageEnglish
Article number93
JournalFrontiers in Plant Science
Volume3
Issue numberMAY
DOIs
Publication statusPublished - 15 May 2012
Externally publishedYes

Keywords

  • Cell expansion
  • Extensins
  • O-glycoproteins
  • O-glycosylation
  • Plant cell wall
  • Proline hydroxylation

ASJC Scopus subject areas

  • Plant Science

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