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

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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. / Lathe, Rahul S.; McFarlane, Heather E.; Kesten, Christopher; Wang, Liu; Khan, Ghazanfar Abbas; Ebert, Berit; Ramírez-Rodríguez, Eduardo Antonio; Zheng, Shuai; Noord, Niels; Frandsen, Kristian; Bhalerao, Rishikesh P.; Persson, Staffan.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 121, No. 15, e2321759121, 2024.

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

Harvard

Lathe, RS, McFarlane, HE, Kesten, C, Wang, L, Khan, GA, Ebert, B, Ramírez-Rodríguez, EA, Zheng, S, Noord, N, Frandsen, K, Bhalerao, RP & Persson, S 2024, 'NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion in Arabidopsis', Proceedings of the National Academy of Sciences of the United States of America, vol. 121, no. 15, e2321759121. https://doi.org/10.1073/pnas.2321759121

APA

Lathe, R. S., McFarlane, H. E., Kesten, C., Wang, L., Khan, G. A., Ebert, B., Ramírez-Rodríguez, E. A., Zheng, S., Noord, N., Frandsen, K., Bhalerao, R. P., & Persson, S. (2024). NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America, 121(15), [e2321759121]. https://doi.org/10.1073/pnas.2321759121

Vancouver

Lathe RS, McFarlane HE, Kesten C, Wang L, Khan GA, Ebert B et al. NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America. 2024;121(15). e2321759121. https://doi.org/10.1073/pnas.2321759121

Author

Lathe, Rahul S. ; McFarlane, Heather E. ; Kesten, Christopher ; Wang, Liu ; Khan, Ghazanfar Abbas ; Ebert, Berit ; Ramírez-Rodríguez, Eduardo Antonio ; Zheng, Shuai ; Noord, Niels ; Frandsen, Kristian ; Bhalerao, Rishikesh P. ; Persson, Staffan. / NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion in Arabidopsis. In: Proceedings of the National Academy of Sciences of the United States of America. 2024 ; Vol. 121, No. 15.

Bibtex

@article{95e7512c3a1c484aafb2ac6bf7753013,
title = "NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion in Arabidopsis",
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.",
keywords = "Arabidopsis, cell biology, cell walls, Golgi apparatus, pectin, Arabidopsis, cell biology, cell walls, Golgi apparatus, pectin",
author = "Lathe, {Rahul S.} and McFarlane, {Heather E.} and Christopher Kesten and Liu Wang and Khan, {Ghazanfar Abbas} and Berit Ebert and Ram{\'i}rez-Rodr{\'i}guez, {Eduardo Antonio} and Shuai Zheng and Niels Noord and Kristian Frandsen and Bhalerao, {Rishikesh P.} and Staffan Persson",
year = "2024",
doi = "10.1073/pnas.2321759121",
language = "English",
volume = "121",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "15",

}

RIS

TY - JOUR

T1 - NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion in Arabidopsis

AU - Lathe, Rahul S.

AU - McFarlane, Heather E.

AU - Kesten, Christopher

AU - Wang, Liu

AU - Khan, Ghazanfar Abbas

AU - Ebert, Berit

AU - Ramírez-Rodríguez, Eduardo Antonio

AU - Zheng, Shuai

AU - Noord, Niels

AU - Frandsen, Kristian

AU - Bhalerao, Rishikesh P.

AU - Persson, Staffan

PY - 2024

Y1 - 2024

N2 - 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.

AB - 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.

KW - Arabidopsis

KW - cell biology

KW - cell walls

KW - Golgi apparatus

KW - pectin

KW - Arabidopsis

KW - cell biology

KW - cell walls

KW - Golgi apparatus

KW - pectin

U2 - 10.1073/pnas.2321759121

DO - 10.1073/pnas.2321759121

M3 - Journal article

C2 - 38579009

AN - SCOPUS:85190353684

VL - 121

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 15

M1 - e2321759121

ER -

ID: 390593570