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 journalJournal articleResearchpeer-review

    46 Citations (Scopus)
    1343 Downloads (Pure)

    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
    Number of pages6
    ISSN1664-462X
    DOIs
    Publication statusPublished - 2012

    Cite this