Filling the Gaps to Solve the Extensin Puzzle

Extensins (EXTs) are highly repetitive plant O-glycoproteins that require several post-translational modifications (PTMs) to become functional in plant cell walls. First, they are hydroxylated on contiguous proline residues; then they are O-glycosylated on hydroxyproline and serine. After secretion...

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Autores principales:	Marzol, E., Borassi, C., Bringas, M., Sede, A., Rodríguez Garcia, D.R., Capece, L., Estevez, J.M.
Formato:	JOUR
Materias:	Arabidopsis thaliana cysteine endopeptidases extensins glycosyltransferases peroxidases prolyl 4-hydroxylases extensin protein, plant glycoprotein plant protein Catharanthus cell membrane metabolism protein processing Cell Membrane Glycoproteins Plant Proteins Protein Processing, Post-Translational
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_16742052_v11_n5_p645_Marzol
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_16742052_v11_n5_p645_Marzol
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spelling	todo:paper_16742052_v11_n5_p645_Marzol2023-10-03T16:29:31Z Filling the Gaps to Solve the Extensin Puzzle Marzol, E. Borassi, C. Bringas, M. Sede, A. Rodríguez Garcia, D.R. Capece, L. Estevez, J.M. Arabidopsis thaliana cysteine endopeptidases extensins glycosyltransferases peroxidases prolyl 4-hydroxylases extensin protein, plant glycoprotein plant protein Catharanthus cell membrane metabolism protein processing Catharanthus Cell Membrane Glycoproteins Plant Proteins Protein Processing, Post-Translational Extensins (EXTs) are highly repetitive plant O-glycoproteins that require several post-translational modifications (PTMs) to become functional in plant cell walls. First, they are hydroxylated on contiguous proline residues; then they are O-glycosylated on hydroxyproline and serine. After secretion into the apoplast, O-glycosylated EXTs form a tridimensional network organized by inter- and intra-Tyr linkages. Recent studies have made significant progress in the identification of the enzymatic machinery required to process EXTs, which includes prolyl 4-hydroxylases, glycosyltransferases, papain-type cysteine endopeptidases, and peroxidases. EXTs are abundant in plant tissues and are particularly important in rapidly expanding root hairs and pollen tubes, which grow in a polar manner. Small changes in EXT PTMs affect fast-growing cells, although the molecular mechanisms underlying this regulation are unknown. In this review, we highlight recent advances in our understanding of EXT modifications throughout the secretory pathway, EXT assembly in cell walls, and possible sensing mechanisms involving the Catharanthus roseus cell surface sensor receptor-like kinases located at the interface between the apoplast and the cytoplasmic side of the plasma membrane. This review describes recent progress in our understanding of extensin post-translational modifications throughout the secretory pathway, extensin secretion and assembly in the cell walls, and possible sensing mechanisms at the interface between the apoplast and the cytoplasmic side of the cell surface. © 2018 The Author JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_16742052_v11_n5_p645_Marzol
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Arabidopsis thaliana cysteine endopeptidases extensins glycosyltransferases peroxidases prolyl 4-hydroxylases extensin protein, plant glycoprotein plant protein Catharanthus cell membrane metabolism protein processing Catharanthus Cell Membrane Glycoproteins Plant Proteins Protein Processing, Post-Translational
spellingShingle	Arabidopsis thaliana cysteine endopeptidases extensins glycosyltransferases peroxidases prolyl 4-hydroxylases extensin protein, plant glycoprotein plant protein Catharanthus cell membrane metabolism protein processing Catharanthus Cell Membrane Glycoproteins Plant Proteins Protein Processing, Post-Translational Marzol, E. Borassi, C. Bringas, M. Sede, A. Rodríguez Garcia, D.R. Capece, L. Estevez, J.M. Filling the Gaps to Solve the Extensin Puzzle
topic_facet	Arabidopsis thaliana cysteine endopeptidases extensins glycosyltransferases peroxidases prolyl 4-hydroxylases extensin protein, plant glycoprotein plant protein Catharanthus cell membrane metabolism protein processing Catharanthus Cell Membrane Glycoproteins Plant Proteins Protein Processing, Post-Translational
description	Extensins (EXTs) are highly repetitive plant O-glycoproteins that require several post-translational modifications (PTMs) to become functional in plant cell walls. First, they are hydroxylated on contiguous proline residues; then they are O-glycosylated on hydroxyproline and serine. After secretion into the apoplast, O-glycosylated EXTs form a tridimensional network organized by inter- and intra-Tyr linkages. Recent studies have made significant progress in the identification of the enzymatic machinery required to process EXTs, which includes prolyl 4-hydroxylases, glycosyltransferases, papain-type cysteine endopeptidases, and peroxidases. EXTs are abundant in plant tissues and are particularly important in rapidly expanding root hairs and pollen tubes, which grow in a polar manner. Small changes in EXT PTMs affect fast-growing cells, although the molecular mechanisms underlying this regulation are unknown. In this review, we highlight recent advances in our understanding of EXT modifications throughout the secretory pathway, EXT assembly in cell walls, and possible sensing mechanisms involving the Catharanthus roseus cell surface sensor receptor-like kinases located at the interface between the apoplast and the cytoplasmic side of the plasma membrane. This review describes recent progress in our understanding of extensin post-translational modifications throughout the secretory pathway, extensin secretion and assembly in the cell walls, and possible sensing mechanisms at the interface between the apoplast and the cytoplasmic side of the cell surface. © 2018 The Author
format	JOUR
author	Marzol, E. Borassi, C. Bringas, M. Sede, A. Rodríguez Garcia, D.R. Capece, L. Estevez, J.M.
author_facet	Marzol, E. Borassi, C. Bringas, M. Sede, A. Rodríguez Garcia, D.R. Capece, L. Estevez, J.M.
author_sort	Marzol, E.
title	Filling the Gaps to Solve the Extensin Puzzle
title_short	Filling the Gaps to Solve the Extensin Puzzle
title_full	Filling the Gaps to Solve the Extensin Puzzle
title_fullStr	Filling the Gaps to Solve the Extensin Puzzle
title_full_unstemmed	Filling the Gaps to Solve the Extensin Puzzle
title_sort	filling the gaps to solve the extensin puzzle
url	http://hdl.handle.net/20.500.12110/paper_16742052_v11_n5_p645_Marzol
work_keys_str_mv	AT marzole fillingthegapstosolvetheextensinpuzzle AT borassic fillingthegapstosolvetheextensinpuzzle AT bringasm fillingthegapstosolvetheextensinpuzzle AT sedea fillingthegapstosolvetheextensinpuzzle AT rodriguezgarciadr fillingthegapstosolvetheextensinpuzzle AT capecel fillingthegapstosolvetheextensinpuzzle AT estevezjm fillingthegapstosolvetheextensinpuzzle
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Filling the Gaps to Solve the Extensin Puzzle

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