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J. Biol. Chem., Vol. 275, Issue 46, 35969-35977, November 17, 2000
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From the The Na,K-ATPase provides the driving force for
many ion transport processes through control of Na+
and K+ concentration gradients across the plasma membranes
of animal cells. It is composed of two subunits, The protein sequence reported in this paper has been submitted to
the Swiss Protein Database under Swiss-Prot accession number P82542.
Identification of a Phospholemman-like Protein from Shark
Rectal Glands
EVIDENCE FOR INDIRECT REGULATION OF Na,K-ATPase BY PROTEIN
KINASE C VIA A NOVEL MEMBER OF THE FXYDY FAMILY*
§,
Department of Biophysics and ¶ Medical
Biochemistry, University of Aarhus, DK-8000 Aarhus C, Denmark
and 
. In many
tissues, predominantly in kidney, it is associated with a small
ancillary component, the 
-subunit that plays a modulatory role. A
novel 15-kDa protein, sharing considerable homology to the -subunit and to phospholemman (PLM) was identified in purified Na,K-ATPase preparations from rectal glands of the shark Squalus
acanthias, but was absent in pig kidney preparations. This
PLM-like protein from shark (PLMS) was found to be a substrate for both
PKA and PKC. Antibodies to the Na,K-ATPase -subunit
coimmunoprecipitated PLMS. Purified PLMS also coimmunoprecipitated with
the -subunit of pig kidney Na,K-ATPase, indicating specific
association with different -isoforms. Finally, PLMS and the
-subunit were expressed in stoichiometric amounts in rectal gland
membrane preparations. Incubation of membrane bound Na,K-ATPase with
non-solubilizing concentrations of C12E8
resulted in functional dissociation of PLMS from Na,K-ATPase and
increased the hydrolytic activity. The same effects were observed after
PKC phosphorylation of Na,K-ATPase membrane preparations. Thus, PLMS
may function as a modulator of shark Na,K-ATPase in a way resembling
the phospholamban regulation of the Ca-ATPase.
*
This work was supported in part by The Danish Biomembrane
Research Center, a University of Aarhus Ph.D. fellowship (to Y. A. M.), The Danish Medical Research Council, and The NOVO
foundations.The costs of publication of this
article were defrayed in part by the
payment of page charges. The 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: Dept. of
Biophysics, Ole Worms Allé 185, University of Aarhus, DK-8000
Aarhus C, Denmark. Tel.: 45-8942-2926; Fax: 45-8612-9599; E-mail:
fc@biophys.au.dk.
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