Source:http://linkedlifedata.com/resource/pubmed/id/11807182
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2002-1-24
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pubmed:abstractText |
The NHE family of ion exchangers includes six isoforms (NHE1-NHE6) that function in an electroneutral exchange of intracellular H(+) for extracellular Na(+). This review focuses on the only ubiquitously expressed isoform, NHE1, which is localized at the plasma membrane where it plays a critical role in intracellular pH (pHi) and cell volume homeostasis. All NHE isoforms share a similar topology: an N-terminus of 12 transmembrane (TM) alpha-helices that collectively function in ion exchange, and a C-terminal cytoplasmic regulatory domain that modulates transport activity by the TM domain. Extracellular signals, mediated by diverse classes of cell-surface receptors, regulate NHE1 activity through distinct signaling networks that converge to directly modify the C-terminal regulatory domain. Modifications in the C-terminus, including phosphorylation and the binding of regulatory proteins, control transport activity by altering the affinity of the TM domain for intracellular H(+). Recently, it was determined that NHE1 also functions as a membrane anchor for the actin-based cytoskeleton, independently of its role in ion translocation. Through its effects on pHi homeostasis, cell volume, and the actin cortical network, NHE1 regulates a number of cell behaviors, including adhesion, shape determination, migration, and proliferation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0362-1642
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
527-52
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading |
pubmed-meshheading:11807182-Animals,
pubmed-meshheading:11807182-Apoptosis,
pubmed-meshheading:11807182-Calmodulin,
pubmed-meshheading:11807182-Cell Division,
pubmed-meshheading:11807182-Cell Survival,
pubmed-meshheading:11807182-Cytoskeleton,
pubmed-meshheading:11807182-Humans,
pubmed-meshheading:11807182-Phosphorylation,
pubmed-meshheading:11807182-Sodium-Hydrogen Antiporter
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pubmed:year |
2002
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pubmed:articleTitle |
The changing face of the Na+/H+ exchanger, NHE1: structure, regulation, and cellular actions.
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pubmed:affiliation |
Department of Stomatology, University of California, San Francisco, HSW 604, San Francisco, California 94143-0512, USA. lputney@itsa.ucsf.edu
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pubmed:publicationType |
Journal Article,
Review
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