Evidence map›Paper›PMID 41083483›Full record

ArticleNPJ systems biology and applications2025

An integrative molecular systems approach unravels mechanisms underlying biphasic nitrate uptake by plant nitrate transporter NRT1.1.

Seemadri Subhadarshini, Sarthak Sahoo, Mohit Kumar Jolly, Mubasher Rashid

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Article in NPJ systems biology and applications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

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2 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Seemadri SubhadarshiniDepartment of Bioengineering, Indian Institute of Science, Bangalore, India. seemadris@iisc.ac.in.
Sarthak SahooDepartment of Bioengineering, Indian Institute of Science, Bangalore, India.
Mohit Kumar JollyDepartment of Bioengineering, Indian Institute of Science, Bangalore, India.
Mubasher RashidDepartment of Mathematics and Statistics, Indian Institute of Technology Kanpur, Kanpur, India. mubasher@iitk.ac.in.

Funding

Department of Science and Technology, Government of India DST/INSPIRE/04/2020/001492Science and Engineering Research Board, Government of India CRG/2023/006432Science and Engineering Research Board, Government of India SB/S2/RJN-049/2018
6 · The paper itself

Abstract

Elucidating the mechanisms of transport kinetics in plants is crucial to develop crops that can use nutrients efficiently. The plant nitrate transporter NRT1.1 rapidly switches between high- and low-affinity transport modes to maintain an optimal uptake amidst fluctuations in nitrate levels. This functional switch is regulated by NRT1.1 phosphorylation, but the precise mechanisms remain poorly understood. Here, using an integrated molecular and systems-level modeling, we identify mechanisms underlying biphasic behaviour of NRT1.1. Phosphorylation of NRT1.1 and its binding to nitrate impacts its overall flexibility and synergistically modulates its global conformation, impacting the nitrate transport rate. Integrating these observations with a regulatory network involving kinases CIPK8/CIPK23 and calcium binding proteins CBL1/9, reveals that in high nitrate conditions, CIPK8-mediated sequestration of CBL1 disrupts the CIPK23-CBL complex required for NRT1.1 phosphorylation, switching NRT1.1 to a low-affinity mode. Together, our findings untangle the molecular complexity enabling NRT1.1 phosphorylation switch with broader implications in nitrate sensing and molecular-level adaption to fluctuating external nutrient levels.

Indexed as

Anion Transport ProteinsNitratesPlant ProteinsArabidopsisArabidopsis ProteinsBiological TransportKineticsNitrate TransportersPhosphorylationSystems BiologyAnion Transport ProteinsArabidopsis ProteinsNitratesNitrate TransportersNRT1.1 protein, ArabidopsisPlant Proteins

Identifiers

PMID41083483
PMCPMC12518564

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