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

doi:10.3389/fpls.2012.00093

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

35 Citationer (Scopus)

966 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.

Originalsprog	Engelsk
Artikelnummer	93
Tidsskrift	Frontiers in Plant Science
Vol/bind	3
Antal sider	6
ISSN	1664-462X
DOI	https://doi.org/10.3389/fpls.2012.00093
Status	Udgivet - 15 maj 2012

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10.3389/fpls.2012.00093

Recent advances on the posttranslational modifications of EXTs and their roles in plant cell wallsForlagets udgivne version, 311 KB

Citationsformater

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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.",

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AU - Salter, Juan Salgado

AU - Dorosz, Javier Gloazzo

AU - Petersen, Bent L

AU - Estevez, José M.

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AB - 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.

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