ArticleBiophysics reports2016
Uniporter substrate binding and transport: reformulating mechanistic questions.
Article in Biophysics reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Structural basis of cytokinin transport by the Arabidopsis AZG2.Nature communications · 2025Article
- Deorphanizing solute carriers inFrontiers in microbiology · 2024Article
- Ins and Outs of Rocker Switch Mechanism in Major Facilitator Superfamily of Transporters.Membranes · 2023Review
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family.Life science alliance · 2021Article
- Thermodynamic secrets of multidrug resistance: A new take on transport mechanisms of secondary active antiporters.Protein science : a publication of the Protein Society · 2018Review
- A critique of the alternating access transporter model of uniport glucose transport.Biophysics reports · 2018Article
- Energy coupling mechanisms of AcrB-like RND transporters.Biophysics reports · 2017Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transporters are involved in material transport, signaling, and energy input in all living cells. One of the fundamental questions about transporters is concerned with the precise role of their substrate in driving the transport process. This is particularly important for uniporters, which must utilize the chemical potential of substrate as the only energy source driving the transport. Thus, uniporters present an excellent model for the understanding of how the difference in substrate concentration across the membrane is used as a driving force. Local conformational changes induced by substrate binding are widely considered as the main mechanism to drive the functional cycle of a transporter; in addition, reducing the energy barrier of the transition state has also been proposed to drive the transporter. However, both points of view require modification to allow consolidation with fundamental thermodynamic principles. Here, we discuss the relationship between thermodynamics and kinetics of uniporters. Substrate binding-induced reduction of the transition-state energy barrier accelerates the transport process in kinetic terms, while the chemical potential of the substrate drives the process thermodynamically.
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