2006
DOI: 10.1074/jbc.m606152200
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Structural and Functional Characterization of Transmembrane Segment VII of the Na+/H+ Exchanger Isoform 1

Abstract: The Na؉ /H ؉ exchanger isoform 1 is an integral membrane protein that regulates intracellular pH by exchanging one intracellular H ؉ for one extracellular Na ؉ . It is composed of an N-terminal membrane domain of 12 transmembrane segments and an intracellular C-terminal regulatory domain. We characterized the structural and functional aspects of the critical transmembrane segment VII (TM VII, residues 251-273) by using alanine scanning mutagenesis and high resolution NMR. Each residue of TM VII was mutated to … Show more

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Cited by 68 publications
(91 citation statements)
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“…The measured IC 50 value for hNHE1 inhibition by EMD87580 was 5 M (Fig. 4C), which is similar to the value reported for wild-type hNHE1 expressed in mammalian cells (39). Fig.…”
Section: Expression Of Human Nhe1 In S Cerevisiae and Preparation Ofsupporting
confidence: 76%
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“…The measured IC 50 value for hNHE1 inhibition by EMD87580 was 5 M (Fig. 4C), which is similar to the value reported for wild-type hNHE1 expressed in mammalian cells (39). Fig.…”
Section: Expression Of Human Nhe1 In S Cerevisiae and Preparation Ofsupporting
confidence: 76%
“…The addition of (NH 4 ) 2 SO 4 completely collapsed the cation gradient across the vesicle membranes and resulted in full recovery of pyranine fluorescence. When vesicles were preincubated with the amiloride analog EMD87580, a potent specific NHE1 inhibitor (39), cation exchange activity of the hNHE1 proteoliposomes was inhibited in a dose-dependent manner (Fig. 4B).…”
Section: Expression Of Human Nhe1 In S Cerevisiae and Preparation Ofmentioning
confidence: 99%
“…3). Extensive mutagenesis within TM5 in NHE1 demonstrated its importance for expression and targeting to the membrane (30), in accordance with its strategic location in the protein core in our model.…”
mentioning
confidence: 56%
“…Some of these mutations do not affect Na ϩ affinity, implying that the inhibitorbinding site is physically distinct and suggesting that the inhibitors induce allosteric regulation (30). FIGURE 4.…”
Section: /Hmentioning
confidence: 99%
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