Chapter 8 Differential Subunit and Isoform Expression Involved in Regulation of Sodium Pump in Skeletal Muscle

Takeyasu, Kunio; Renaud, K J; Taormino, J P; Wolitzky, Barry A.; Barnstein, Andrew M.; Tamkun, Michael M.; Fambrough, Douglas M.

doi:10.1016/s0070-2161(08)60012-x

Cited by 52 publications

(24 citation statements)

References 34 publications

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“…First, whether heterogeneity of the&subunits exists at the protein level, apart from the heterogeneity of glycosylation. &Subunit mRNAs from different sources (Torpedo [17], sheep, pig, dog and chicken [18,19,22,23], human HeLa cells [20], rat [21,83]) are cloned. In each case only the coding sequence was found.…”

Section: The Family Of ~-Subunit Genesmentioning

confidence: 99%

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Broude¹,

Modyanov²,

Monastyrskaya³

1989

FEBS Letters

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Complete primary stators of both submit of Na',K+-ATPase from various sources have been ~~biisbed by a ~mbination of the methods for molecular cloning and protein chemistry. The gene family homologo~ to the a-subunit cDNA of animal Na+,K*-ATPases has been found in the human genome. Some genes of this family encode the known isoforms (aI and aI1) of the Na+,K+-ATPase catalytic subunit. The proteins coded by other genes can be either new isoforms of the Na+,K+-ATPase catalytic subunit or other ion-transporting ATPases. Expression of the genes of this family proceeds in a tissue-specific manner and changes during the postnatal development and neoplastic transformation. The complete exon-intron structure of one of the genes of this family has been established. This gene codes for the form of the catalytic subunit, the existence of which has been unknown. Apparently, all the genes of the discovered family have a similar intron-exon structure. There is certain correlation between the gene structure and the proposed domain a~angement of the a-subunit. The results obtained have become the basis for the experiments which prove the existence of the earlier unknown afI1 isoform of the Na+,K+-ATPase catalytic subunit and have made possible the study of its function.

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Section: The Family Of ~-Subunit Genesmentioning

confidence: 99%

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Broude¹,

Modyanov²,

Monastyrskaya³

1989

FEBS Letters

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“…Although the reason for the importance of the Cys16'-cys'76 and Cys 215-Cys278 loops, for the assembly is not yet known, it is to be noted that the sequences of these loops in isoform bl of the B-subunit are significantly conserved among Torpedo [ 161, human [ 191, sheep [20], dog [21], pig [22], rat [23], chicken [24] and Xenopus [25]. It can bee seen in Fig.…”

Section: Discussionmentioning

confidence: 99%

The functional roles of disulfide bonds in the β‐subunit of (Na,K)ATPase as studied by site‐directed mutagenesis

1994

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The /I-subunit of Torpedo californica (Na,K)ATPase contains seven cysteine residues; one (Cysti) is in the single transmembrane segment and the other six (CYS'*~, Cys'%, Cys'@', CYS'~~, Cys"' and Cysz7*) are in the extracellular domain and form three highly conserved disulfide bonds. A/?-subunit mutant with replacement of Cy@ by Ser could assemble with the a-subunit, and the resulting a&complex was catalytically active. Mutants in which either the N-terminal side or both Cys residues of the Cys"%ys Iso bond were replaced by Ser could also tightly assemble with the a-subunit, but the resulting @complex was catalytically inactive. On the other hand, disruption of either the Cy~'~-Cys'~~ or Cy~~'~-Cys~~s bond by substituting the N-terminal side only or both Cys residues with Ser led to aSsubunit that could not assemble with the u-subunit. We conclude that the structure of the @ubunit around the Cy~'~Cys'~~ and Cy~~'~-Cys 27* loops is indispensable for assembly with the u-subunit, whereas the Cy~'~~-Cys'~~ loop is not essential for assembly but is required for enzyme activity.

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“…Included mto the search are the followmg rat NKAl-3, three lsoforms of rat bram Na,K-ATPase a-subumt [l], TorpCal NK, asubunit of the Torpedo calrfornrca electroplax Na,K-ATPase [13], chlcken NK, Lu-subumt of the chlcken kidney Na,K-ATPase [14]; sheep NK, cY-subunit of the sheep kidney Na,K-ATPase [15], pig NK, cu-subunit of the pig kidney Na,K-ATPase [16], human NK, Usubumt of HeLa cell Na,K-ATPase [17], yeast PMAl, plasma membrane ATPase of yeast [18], E C KdbB, K-transport ATPase of E co/r [19], SRst Ca and SRft Ca, sarcoplasmlc reticulum CaATPases of slow twitch and of fast twitch rabbit muscle cells, respectively [2], PM Cal and PM Ca2, two lsoforms of the rat bram plasma membrane Ca-ATPase [3] The rat Na,K-ATPase cYl-subumt numbering IS used * and P Indicate the Asp residue phosphorylated, * and F the Lys residue covalently labelled by fluorescent lsothlocyanate (FITC), respectively Segments of the consensus sequences consldered for primer design are underhned Genomlc DNA was dlgested with restrIctIon enzymes BarnHI, EcoRI and HtndIII The dlgestlon products were fractionated on a 0 8% agarose gel, transferred to mtrocellulose paper and probed High strmgency wash (65°C) has been applied.…”

Section: Fig 1 Design Of the Pcr-pnmers Members Of The Atpase Familymentioning

confidence: 99%

Amplification of the phosphorylation site ‐ ATP‐binding site cDNA fragment of the Na⁺,K⁺‐ATPase and the Ca²⁺‐ATPase of Drosophila melanogaster by polymerase chain reaction

1989

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In vitro ~NA-arnp~l~cation techmque has been utdmed to generate a 430 bp fragment of the Na+,K+-ATPase, and a 550 bp fragment of a Ca2+-ATPase (the sarcoplasmtc reticulum-type) of Drosoph&~ melunogaster The ohgonucleotrde prtmers for the DNA-ampbficatton (Polymerase Cham Reaction) had been desrgned on the basis of ammo acid sequence motifs -the phosphorylatton site and the ATP-bmdmg sate -conserved among members of the ATPase protein famdy Usmg the amphfied cDNA-segments as probes, we demonstrated that there IS one Na+,K+-ATPase and one CaZ+-ATPase (sarcoplasmrc rettculum-type) gene m the Drosophda genome Three dtfferent mRNA species are processed from the Na+,K+-ATPase gene and one from the Ca s+-ATPase gene Developmental control m expression of the Ca2+-ATPase gene was observed Homology pnmer, Polymerase chain reaction, ATPase, Deveiopmental control of gene expresston, (Drasaph~~u me~~ag~ter)

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Chapter 8 Differential Subunit and Isoform Expression Involved in Regulation of Sodium Pump in Skeletal Muscle

Cited by 52 publications

References 34 publications

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

The functional roles of disulfide bonds in the β‐subunit of (Na,K)ATPase as studied by site‐directed mutagenesis

Amplification of the phosphorylation site ‐ ATP‐binding site cDNA fragment of the Na⁺,K⁺‐ATPase and the Ca²⁺‐ATPase of Drosophila melanogaster by polymerase chain reaction

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Chapter 8 Differential Subunit and Isoform Expression Involved in Regulation of Sodium Pump in Skeletal Muscle

Cited by 52 publications

References 34 publications

Advances in Na+,K+‐ATPase studies: from protein to gene and back to protein

Advances in Na+,K+‐ATPase studies: from protein to gene and back to protein

The functional roles of disulfide bonds in the β‐subunit of (Na,K)ATPase as studied by site‐directed mutagenesis

Amplification of the phosphorylation site ‐ ATP‐binding site cDNA fragment of the Na+,K+‐ATPase and the Ca2+‐ATPase of Drosophila melanogaster by polymerase chain reaction

Contact Info

Product

Resources

About

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Amplification of the phosphorylation site ‐ ATP‐binding site cDNA fragment of the Na⁺,K⁺‐ATPase and the Ca²⁺‐ATPase of Drosophila melanogaster by polymerase chain reaction