ReviewThe Biochemical journal2001
Functional role of polar amino acid residues in Na+/H+ exchangers.
Review in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 66 citations in OpenAlex.
- ZxNHX1 from a xerophyte outperforms AtNHX1 in sequestering NaPlant biotechnology journal · 2025Article
- Searching for genes determining the APR phenotype in rye.BMC plant biology · 2025Article
- Variations in exons 11 and 12 of the multi-pest resistance wheat geneFrontiers in plant science · 2022Article
- Plant nitrogen uptake and assimilation: regulation of cellular pH homeostasis.Journal of experimental botany · 2020Review
- Functional role and analysis of cysteine residues of the salt tolerance protein Sod2.Molecular and cellular biochemistry · 2014Article
- Structural and functional analysis of transmembrane segment IV of the salt tolerance protein Sod2.The Journal of biological chemistry · 2013Article
- Salt overly sensitive pathway members are influenced by diurnal rhythm in rice.Plant signaling & behavior · 2013Article
- PvAMT1;1, a highly selective ammonium transporter that functions as H+/NH4(+) symporter.The Journal of biological chemistry · 2011Article
- Conserved charged amino acid residues in the extracellular region of sodium/iodide symporter are critical for iodide transport activity.Journal of biomedical science · 2010Article
- A novel plant vacuolar Na+/H+ antiporter gene evolved by DNA shuffling confers improved salt tolerance in yeast.The Journal of biological chemistry · 2010Article
- Evidence that highly conserved residues of transmembrane segment 6 of Escherichia coli MntH are important for transport activity.Biochemistry · 2010Article
- Shewanella spp. genomic evolution for a cold marine lifestyle and in-situ explosive biodegradation.PloS one · 2010Article
- The role of annexin 1 in drought stress in Arabidopsis.Plant physiology · 2009Article
- Expression, purification, and reconstitution of the Na(+)/H (+) exchanger sod2 in Saccharomyces cerevisiae.Molecular and cellular biochemistry · 2008Article
- Structural and functional analysis of the Na+/H+ exchanger.The Biochemical journal · 2007Review
- Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and System N (SNAT5) amino acid transporter activity involving a conserved histidine residue.The Biochemical journal · 2006Article
- Identification of a pH sensor in the furin propeptide that regulates enzyme activation.The Journal of biological chemistry · 2006Article
- The conserved histidine 295 does not contribute to proton cotransport by the glutamate transporter EAAC1.Biochemistry · 2005Article
- Identification of conserved polar residues important for salt tolerance by the Na+/H+ exchanger of Schizosaccharomyces pombe.Molecular and cellular biochemistry · 2005Article
- Metabolic interdependence of obligate intracellular bacteria and their insect hosts.Microbiology and molecular biology reviews : MMBR · 2004Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Na(+)/H(+) exchangers are a family of ubiquitous membrane proteins. In higher eukaryotes they regulate cytosolic pH by removing an intracellular H(+) in exchange for an extracellular Na(+). In yeast and Escherichia coli, Na(+)/H(+) exchangers function in the opposite direction to remove intracellular Na(+) in exchange for extracellular H(+). Na(+)/H(+) exchangers display an internal pH-sensitivity that varies with the different antiporter types. Only recently have investigations examined the amino acids involved in pH-sensitivity and in cation binding and transport. Histidine residues are good candidates for H(+)-sensing amino acids, since they can ionize within the physiological pH range. Histidine residues have been shown to be important in the function of the E. coli Na(+)/H(+) exchanger NhaA and in the yeast Na(+)/H(+) exchanger sod2. In E. coli, His(225) of NhaA may function to interact with, or regulate, the pH-sensory region of NhaA. In sod2, His(367) is also critical to transport and may be a functional analogue of His(225) of NhaA. Histidine residues are not critical for the function of the mammalian Na(+)/H(+) exchanger, although an unusual histidine-rich sequence of the C-terminal tail has some influence on activity. Other amino acids involved in cation binding and transport by Na(+)/H(+) exchangers are only beginning to be studied. Amino acids with polar side chains such as aspartate and glutamate have been implicated in transport activity of NhaA and sod2, but have not been studied in the mammalian Na(+)/H(+) exchanger. Further studies are needed to elucidate the mechanisms involved in pH-sensitivity and cation binding and transport by Na(+)/H(+) exchangers.
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