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Originally published In Press as doi:10.1074/jbc.M305126200 on July 21, 2003

J. Biol. Chem., Vol. 278, Issue 39, 37427-37438, September 26, 2003
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Regulation of Na,K-ATPase by PLMS, the Phospholemman-like Protein from Shark

MOLECULAR CLONING, SEQUENCE, EXPRESSION, CELLULAR DISTRIBUTION, AND FUNCTIONAL EFFECTS OF PLMS*

Yasser A. Mahmmoud {ddagger}, Gordon Cramb §, Arvid B Maunsbach ¶, Christopher P. Cutler §, Lara Meischke § and Flemming Cornelius {ddagger} ||

From the {ddagger}Department of Biophysics, University of Aarhus, Ole Worms Allé 185, DK-8000 Aarhus C, Denmark, The Water and Salt Research Centre, Department of Cell Biology, Institute of Anatomy, University of Aarhus, DK-8000 Aarhus C, Denmark, and the §School of Biology, Bute Medical Bldgs., University of St-Andrews, Fife KY16 9TS, United Kingdom

In Na,K-ATPase membrane preparations from shark rectal glands, we have previously identified an FXYD domain-containing protein, phospholemman-like protein from shark, PLMS. This protein was shown to associate and modulate shark Na,K-ATPase activity in vitro. Here we describe the complete coding sequence, expression, and cellular localization of PLMS in the rectal gland of the shark Squalus acanthias. The mature protein contained 74 amino acids, including the N-terminal FXYD motif and a C-terminal protein kinase multisite phosphorylation motif. The sequence is preceded by a 20 amino acid candidate cleavable signal sequence. Immunogold labeling of the Na,K-ATPase {alpha}-subunit and PLMS showed the presence of {alpha} and PLMS in the basolateral membranes of the rectal gland cells and suggested their partial colocalization. Furthermore, through controlled proteolysis, the C terminus of PLMS containing the protein kinase phosphorylation domain can be specifically cleaved. Removal of this domain resulted in stimulation of maximal Na,K-ATPase activity, as well as several partial reactions. Both the E1~P -> E2-P reaction, which is partially rate-limiting in shark, and the K+ deocclusion reaction, E2(K) -> E1, are accelerated. The latter may explain the finding that the apparent Na+ affinity was increased by the specific C-terminal PLMS truncation. Thus, these data are consistent with a model where interaction of the phosphorylation domain of PLMS with the Na,K-ATPase {alpha}-subunit is important for the modulation of shark Na,K-ATPase activity.

Received for publication, May 15, 2003 , and in revised form, July 14, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AJ556170.

* This work was supported by the Danish Medical Research Council, Aarhus University Research Foundation, the A. P. Møller foundation, The Novo Nordic Foundation (to F. C. and Y. A. M.), and The Danish Natural Research Foundation (to A. B. M.). The Federation of the European Biochemical Societies (FEBS) is acknowledged for providing an FEBS summer fellowship (to Y. A. M.) to perform the cloning work. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed. Tel.: 45-8942-2926; Fax: 45-8612-9599; E-mail: fc{at}biophys.au.dk.


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