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

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Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls. / Velasquez, Melina; Salter, Juan Salgado; Dorosz, Javier Gloazzo; Petersen, Bent L; Estevez, José M.

In: Frontiers in Plant Science, Vol. 3, 93, 2012.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Velasquez, M, Salter, JS, Dorosz, JG, Petersen, BL & Estevez, JM 2012, 'Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls', Frontiers in Plant Science, vol. 3, 93. https://doi.org/10.3389/fpls.2012.00093

APA

Velasquez, M., Salter, J. S., Dorosz, J. G., Petersen, B. L., & Estevez, J. M. (2012). Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls. Frontiers in Plant Science, 3, [93]. https://doi.org/10.3389/fpls.2012.00093

Vancouver

Velasquez M, Salter JS, Dorosz JG, Petersen BL, Estevez JM. Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls. Frontiers in Plant Science. 2012;3. 93. https://doi.org/10.3389/fpls.2012.00093

Author

Velasquez, Melina ; Salter, Juan Salgado ; Dorosz, Javier Gloazzo ; Petersen, Bent L ; Estevez, José M. / Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls. In: Frontiers in Plant Science. 2012 ; Vol. 3.

Bibtex

@article{8b0782b03d524157802270d774737e30,
title = "Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls",
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.",
author = "Melina Velasquez and Salter, {Juan Salgado} and Dorosz, {Javier Gloazzo} and Petersen, {Bent L} and Estevez, {Jos{\'e} M.}",
year = "2012",
doi = "10.3389/fpls.2012.00093",
language = "English",
volume = "3",
journal = "Frontiers in Plant Science",
issn = "1664-462X",
publisher = "Frontiers Media S.A.",

}

RIS

TY - JOUR

T1 - Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls

AU - Velasquez, Melina

AU - Salter, Juan Salgado

AU - Dorosz, Javier Gloazzo

AU - Petersen, Bent L

AU - Estevez, José M.

PY - 2012

Y1 - 2012

N2 - 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.

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.

U2 - 10.3389/fpls.2012.00093

DO - 10.3389/fpls.2012.00093

M3 - Journal article

C2 - 22639676

VL - 3

JO - Frontiers in Plant Science

JF - Frontiers in Plant Science

SN - 1664-462X

M1 - 93

ER -

ID: 49642234