C1A cysteine protease-cystatin interactions in leaf senescence

© The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Détails bibliographiques
Publié dans:Journal of experimental botany. - 1985. - 65(2014), 14 vom: 18. Juli, Seite 3825-33
Auteur principal: Díaz-Mendoza, Mercedes (Auteur)
Autres auteurs: Velasco-Arroyo, Blanca, González-Melendi, Pablo, Martínez, Manuel, Díaz, Isabel
Format: Article en ligne
Langue:English
Publié: 2014
Accès à la collection:Journal of experimental botany
Sujets:Journal Article Research Support, Non-U.S. Gov't Review Cystatin cysteine protease leaf senescence nutrient recycling protein breakdown proteolysis. Cystatins plus... Plant Proteins Cysteine Proteases EC 3.4.-
Description
Résumé:© The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
Senescence-associated proteolysis in plants is a crucial process to relocalize nutrients from leaves to growing or storage tissues. The massive net degradation of proteins involves broad metabolic networks, different subcellular compartments, and several types of proteases and regulators. C1A cysteine proteases, grouped as cathepsin L-, B-, H-, and F-like according to their gene structures and phylogenetic relationships, are the most abundant enzymes responsible for the proteolytic activity during leaf senescence. Besides, cystatins as specific modulators of C1A peptidase activities exert a complex regulatory role in this physiological process. This overview article covers the most recent information on C1A proteases in leaf senescence in different plant species. Particularly, it is focussed on barley, as the unique species where the whole gene family members of C1A cysteine proteases and cystatins have been analysed
Description:Date Completed 30.03.2015
Date Revised 18.03.2022
published: Print-Electronic
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/eru043