A cluster of cytoplasmic histidine residues specifies pH dependence of the AE2 plasma membrane anion exchanger

Israel Sekler; Sumire Kobayashi; Ron R. Kopito

doi:10.1016/S0092-8674(00)80168-3

A cluster of cytoplasmic histidine residues specifies pH dependence of the AE2 plasma membrane anion exchanger

Israel Sekler, Sumire Kobayashi, Ron R. Kopito

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Intracellular pH is maintained by a dynamic equilibrium balancing the opposing forces of proton loading and proton extrusion. By providing an efflux pathway for base, anion exchangers constitute a key component of the plasma membrane proton-loading machinery. The data in this paper identify a histidine-rich sequence within the cytoplasmic domain of the nonerythroid anion exchanger, AE2, that serves as an intracellular pH 'sensor' that modulates anion exchange activity within the physiological range of cytoplasmic pH. These data reveal an interaction between the two major domains of the anion exchanger and suggest a novel substrate feedback mechanism by which intracellular protons directly control the activity of an acid-loading plasma membrane ion transporter.

Original language	English
Pages (from-to)	929-935
Number of pages	7
Journal	Cell
Volume	86
Issue number	6
DOIs	https://doi.org/10.1016/S0092-8674(00)80168-3
State	Published - 20 Sep 1996
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/S0092-8674(00)80168-3

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title = "A cluster of cytoplasmic histidine residues specifies pH dependence of the AE2 plasma membrane anion exchanger",

abstract = "Intracellular pH is maintained by a dynamic equilibrium balancing the opposing forces of proton loading and proton extrusion. By providing an efflux pathway for base, anion exchangers constitute a key component of the plasma membrane proton-loading machinery. The data in this paper identify a histidine-rich sequence within the cytoplasmic domain of the nonerythroid anion exchanger, AE2, that serves as an intracellular pH 'sensor' that modulates anion exchange activity within the physiological range of cytoplasmic pH. These data reveal an interaction between the two major domains of the anion exchanger and suggest a novel substrate feedback mechanism by which intracellular protons directly control the activity of an acid-loading plasma membrane ion transporter.",

author = "Israel Sekler and Sumire Kobayashi and Kopito, {Ron R.}",

note = "Funding Information: Correspondence should be addressed to R. R. K. The authors wish to thank Ms. Lex Bunten for expert editorial and administrative help. This work was supported by a grant from the National Institutes of Health (GM38543) and was performed during the tenure of an Established Investigatorship of the American Heart Association (R. R. K.).",

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T1 - A cluster of cytoplasmic histidine residues specifies pH dependence of the AE2 plasma membrane anion exchanger

AU - Sekler, Israel

AU - Kobayashi, Sumire

AU - Kopito, Ron R.

N1 - Funding Information: Correspondence should be addressed to R. R. K. The authors wish to thank Ms. Lex Bunten for expert editorial and administrative help. This work was supported by a grant from the National Institutes of Health (GM38543) and was performed during the tenure of an Established Investigatorship of the American Heart Association (R. R. K.).

PY - 1996/9/20

Y1 - 1996/9/20

N2 - Intracellular pH is maintained by a dynamic equilibrium balancing the opposing forces of proton loading and proton extrusion. By providing an efflux pathway for base, anion exchangers constitute a key component of the plasma membrane proton-loading machinery. The data in this paper identify a histidine-rich sequence within the cytoplasmic domain of the nonerythroid anion exchanger, AE2, that serves as an intracellular pH 'sensor' that modulates anion exchange activity within the physiological range of cytoplasmic pH. These data reveal an interaction between the two major domains of the anion exchanger and suggest a novel substrate feedback mechanism by which intracellular protons directly control the activity of an acid-loading plasma membrane ion transporter.

AB - Intracellular pH is maintained by a dynamic equilibrium balancing the opposing forces of proton loading and proton extrusion. By providing an efflux pathway for base, anion exchangers constitute a key component of the plasma membrane proton-loading machinery. The data in this paper identify a histidine-rich sequence within the cytoplasmic domain of the nonerythroid anion exchanger, AE2, that serves as an intracellular pH 'sensor' that modulates anion exchange activity within the physiological range of cytoplasmic pH. These data reveal an interaction between the two major domains of the anion exchanger and suggest a novel substrate feedback mechanism by which intracellular protons directly control the activity of an acid-loading plasma membrane ion transporter.

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A cluster of cytoplasmic histidine residues specifies pH dependence of the AE2 plasma membrane anion exchanger

Abstract

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