Home > Publications database > Assembly of retinal rod or cone Na+/Ca2+/K+-exchanger oligomers with cGMP-gated channel subunits as probed with heterologously expressed cDNAs > print

001     30216
005     20200423203517.0
024 7 _ |a pmid:12693957
|2 pmid
024 7 _ |a 10.1021/bi027276z
|2 DOI
024 7 _ |a WOS:000182420000031
|2 WOS
024 7 _ |a 2128/671
|2 Handle
024 7 _ |a altmetric:3547932
|2 altmetric
037 _ _ |a PreJuSER-30216
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Kang, K.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Assembly of retinal rod or cone Na+/Ca2+/K+-exchanger oligomers with cGMP-gated channel subunits as probed with heterologously expressed cDNAs
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2003
300 _ _ |a 4593 - 4600
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Biochemistry
|x 0006-2960
|0 798
|v 42
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Proper control of intracellular free Ca(2+) is thought to involve subsets of proteins that co-localize to mediate coordinated Ca(2+) entry and Ca(2+) extrusion. The outer segments of vertebrate rod and cone photoreceptors present one example: Ca(2+) influx is exclusively mediated via cGMP-gated channels (CNG), whereas the Na(+)/Ca(2+)-K(+) exchanger (NCKX) is the only Ca(2+) extrusion protein present. In situ, a rod NCKX homodimer and a CNG heterotetramer are thought to be part of a single protein complex. However, NCKX-NCKX and NCKX-CNG interactions have been described so far only in bovine rod outer segment membranes. We have used thiol-specific cross-linking and co-immunoprecipitation to examine NCKX self-assembly and CNG-NCKX co-assembly after heterologous expression of either the rod or cone NCKX/CNG isoforms. Co-immunoprecipitation clearly demonstrated both NCKX homooligomerization and interactions between NCKX and CNG. The NCKX-NCKX and NCKX-CNG interactions were observed for both the rod and the cone isoforms. Thiol-specific cross-linking led to rod NCKX1 dimers and to cone NCKX2 adducts of an apparent molecular weight higher than that predicted for a NCKX2 dimer. The mass of the cross-link product critically depended on the location of the particular cysteine residue used by the cross-linker, and we cannot exclude that NCKX forms a higher oligomer. The NCKX-NCKX and NCKX-CNG interactions were not isoform-specific (i.e., rod NCKX could interact with cone NCKX, rod NCKX could interact with cone CNGA, and vice versa). Deletion of the two large hydrophilic loops from the NCKX protein did not abolish the NCKX oligomerization, suggesting that it is mediated by the highly conserved transmembrane spanning segments.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Calcium: metabolism
650 _ 2 |2 MeSH
|a Cell Line
650 _ 2 |2 MeSH
|a Chickens: metabolism
650 _ 2 |2 MeSH
|a Cyclic GMP: metabolism
650 _ 2 |2 MeSH
|a Cyclic Nucleotide-Gated Cation Channels
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Insects
650 _ 2 |2 MeSH
|a Ion Channels: metabolism
650 _ 2 |2 MeSH
|a Photoreceptor Cells, Vertebrate: metabolism
650 _ 2 |2 MeSH
|a Precipitin Tests
650 _ 2 |2 MeSH
|a Sodium-Calcium Exchanger: biosynthesis
650 _ 2 |2 MeSH
|a Sodium-Calcium Exchanger: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Cyclic Nucleotide-Gated Cation Channels
650 _ 7 |0 0
|2 NLM Chemicals
|a Ion Channels
650 _ 7 |0 0
|2 NLM Chemicals
|a Sodium-Calcium Exchanger
650 _ 7 |0 147478-17-9
|2 NLM Chemicals
|a potassium-dependent sodium-calcium exchanger
650 _ 7 |0 7440-70-2
|2 NLM Chemicals
|a Calcium
650 _ 7 |0 7665-99-8
|2 NLM Chemicals
|a Cyclic GMP
650 _ 7 |a J
|2 WoSType
700 1 _ |a Bauer, P. J.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB4672
700 1 _ |a Kinjo, T. G.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Szerencsei, R. T.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Bönigk, W.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB22199
700 1 _ |a Winkfein, R. J.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Schnetkamp, P. P. M.
|b 6
|0 P:(DE-HGF)0
773 _ _ |a 10.1021/bi027276z
|g Vol. 42, p. 4593 - 4600
|p 4593 - 4600
|q 42<4593 - 4600
|0 PERI:(DE-600)1472258-6
|t Biochemistry
|v 42
|y 2003
|x 0006-2960
856 7 _ |u http://dx.doi.org/10.1021/bi027276z
|u http://hdl.handle.net/2128/671
856 4 _ |u https://juser.fz-juelich.de/record/30216/files/27726.pdf
|y OpenAccess
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|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:30216
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913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
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914 1 _ |y 2003
915 _ _ |0 StatID:(DE-HGF)0010
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920 1 _ |k IBI-1
|l Zelluläre Signalverarbeitung
|d 31.12.2006
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