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

被引:108
作者
Mahmmoud, YA [1 ]
Vorum, H [1 ]
Cornelius, F [1 ]
机构
[1] Aarhus Univ, Dept Biophys, DK-8000 Aarhus C, Denmark
关键词
D O I
10.1074/jbc.M005168200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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, cu and beta, In many tissues, predominantly in kidney, it is associated with a small ancillary component, the gamma -subunit that plays a modulatory role. A novel 15-kDa protein, sharing considerable homology to the gamma -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 or subunit coimmunoprecipitated PLMS, Purified PLMS also coimmunoprecipitated with the ol-subunit of pig kidney Na,K-ATPase, indicating specific association with different alpha -isoforms. Finally, PLMS and the alpha -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.
引用
收藏
页码:35969 / 35977
页数:9
相关论文
共 54 条
[1]   The γ subunit modulates Na+ and K+ affinity of the renal Na,K-ATPase [J].
Arystarkhova, E ;
Wetzel, RK ;
Asinovski, NK ;
Sweadner, KJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (47) :33183-33185
[2]   A CORTICOSTEROID-INDUCED GENE EXPRESSING AN ISK-LIKE K+ CHANNEL ACTIVITY IN XENOPUS OOCYTES [J].
ATTALI, B ;
LATTER, H ;
RACHAMIM, N ;
GARTY, H .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (13) :6092-6096
[3]   β-subunit assembly is essential for the correct packing and the stable membrane insertion of the H,K-ATPase α-subunit [J].
Beggah, AT ;
Béguin, P ;
Bamberg, K ;
Sachs, G ;
Geering, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (12) :8217-8223
[4]  
BEGUIN P, 1994, J BIOL CHEM, V269, P24437
[5]   The gamma subunit is a specific component of the Na,K-ATPase and modulates its transport function [J].
Beguin, P ;
Wang, XY ;
Firsov, D ;
Puoti, A ;
Claeys, D ;
Horisberger, JD ;
Geering, K .
EMBO JOURNAL, 1997, 16 (14) :4250-4260
[6]  
Celis JE, 1998, CELL BIOLOGY - A LABOARATORY HANDBOOK, 2ND EDITION, VOL 4, P404
[7]  
CELIS JE, 1994, CELL BIOL LABORATORY, V3, P222
[8]   Characterization of the human and rat phospholemman (PLM) cDNAs and localization of the human PLM gene to chromosome 19q13.1 [J].
Chen, LSK ;
Lo, CF ;
Numann, R ;
Cuddy, M .
GENOMICS, 1997, 41 (03) :435-443
[9]   Structural domains in phospholemman - A possible role for the carboxyl terminus in channel inactivation [J].
Chen, ZH ;
Jones, LR ;
O'Brian, JJ ;
Moorman, JR ;
Cala, SE .
CIRCULATION RESEARCH, 1998, 82 (03) :367-374
[10]  
CLELAND WW, 1963, BIOCHIM BIOPHYS ACTA, V67, P188