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NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion in Arabidopsis.

Authors :
Lathe, Rahul S.
McFarlane, Heather E.
Kesten, Christopher
Liu Wang
Khan, Ghazanfar Abbas
Ebert, Berit
Antonio Ramírez-Rodríguez, Eduardo
Shuai Zheng
Noord, Niels
Frandsen, Kristian
Bhalerao, Rishikesh P.
Persson, Staffan
Source :
Proceedings of the National Academy of Sciences of the United States of America; 4/9/2024, Vol. 121 Issue 15, p1-11, 44p
Publication Year :
2024

Abstract

Adjacent plant cells are connected by specialized cell wall regions, called middle lamellae, which influence critical agricultural characteristics, including fruit ripening and organ abscission. Middle lamellae are enriched in pectin polysaccharides, specifically homogalacturonan (HG). Here, we identify a plant-specific Arabidopsis DUF1068 protein, called NKS1/ELMO4, that is required for middle lamellae integrity and cell adhesion. NKS1 localizes to the Golgi apparatus and loss of NKS1 results in changes to Golgi structure and function. The nks1 mutants also display HG deficient phenotypes, including reduced seedling growth, changes to cell wall composition, and tissue integrity defects. These phenotypes are comparable to qua1 and qua2 mutants, which are defective in HG biosynthesis. Notably, genetic interactions indicate that NKS1 and the QUAs work in a common pathway. Protein interaction analyses and modeling corroborate that they work together in a stable protein complex with other pectin-related proteins. We propose that NKS1 is an integral part of a large pectin synthesis protein complex and that proper function of this complex is important to support Golgi structure and function. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00278424
Volume :
121
Issue :
15
Database :
Complementary Index
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Publication Type :
Academic Journal
Accession number :
176602410
Full Text :
https://doi.org/10.1073/pnas.2321759121