Linked Life Data

17606467

Source:http://linkedlifedata.com/resource/pubmed/id/17606467

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2007-10-1
pubmed:abstractText
We characterized a family consisting of four mammalian proteins of unknown function (NKAIN1, 2, 3 and 4) and a single Drosophila ortholog dNKAIN. Aside from highly conserved transmembrane domains, NKAIN proteins contain no characterized functional domains. Striking amino acid conservation in the first two transmembrane domains suggests that these proteins are likely to function within the membrane bilayer. NKAIN family members are neuronally expressed in multiple regions of the mouse brain, although their expression is not ubiquitous. We demonstrate that mouse NKAIN1 interacts with the beta1 subunit of the Na,K-ATPase, whereas Drosophila ortholog dNKAIN interacts with Nrv2.2, a Drosophila homolog of the Na,K-ATPase beta subunits. We also show that NKAIN1 can form a complex with another beta subunit-binding protein, MONaKA, when binding to the beta1 subunit of the Na,K-ATPase. Our results suggest that a complex between mammalian NKAIN1 and MONaKA is required for NKAIN function, which is carried out by a single protein, dNKAIN, in Drosophila. This hypothesis is supported by the fact that dNKAIN, but not NKAIN1, induces voltage-independent amiloride-insensitive Na(+)-specific conductance that can be blocked by lanthanum. Drosophila mutants with decreased dNKAIN expression due to a P-element insertion in the dNKAIN gene exhibit temperature-sensitive paralysis, a phenotype also caused by mutations in the Na,K-ATPase alpha subunit and several ion channels. The neuronal expression of NKAIN proteins, their membrane localization and the temperature-sensitive paralysis of NKAIN Drosophila mutants strongly suggest that this novel protein family may be critical for neuronal function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0964-6906
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2394-410
pubmed:meshHeading
pubmed-meshheading:17606467-Amino Acid Sequence, pubmed-meshheading:17606467-Animals, pubmed-meshheading:17606467-Animals, Genetically Modified, pubmed-meshheading:17606467-Base Sequence, pubmed-meshheading:17606467-Brain, pubmed-meshheading:17606467-Carrier Proteins, pubmed-meshheading:17606467-Cells, Cultured, pubmed-meshheading:17606467-Conserved Sequence, pubmed-meshheading:17606467-Drosophila, pubmed-meshheading:17606467-Female, pubmed-meshheading:17606467-Humans, pubmed-meshheading:17606467-Male, pubmed-meshheading:17606467-Membrane Proteins, pubmed-meshheading:17606467-Models, Biological, pubmed-meshheading:17606467-Molecular Sequence Data, pubmed-meshheading:17606467-Multigene Family, pubmed-meshheading:17606467-Nerve Tissue Proteins, pubmed-meshheading:17606467-Neurons, pubmed-meshheading:17606467-Protein Binding, pubmed-meshheading:17606467-Protein Structure, Tertiary, pubmed-meshheading:17606467-Protein Subunits, pubmed-meshheading:17606467-Sequence Homology, Amino Acid, pubmed-meshheading:17606467-Sodium-Potassium-Exchanging ATPase, pubmed-meshheading:17606467-Transfection
pubmed:year
2007
pubmed:articleTitle
A novel family of transmembrane proteins interacting with beta subunits of the Na,K-ATPase.
pubmed:affiliation
Laboratory of Molecular Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural