Literature DB >> 2545189

Regulation of the Ca2+ pump ATPase by cAMP-dependent phosphorylation of phospholamban.

M Tada, M Kadoma.   

Abstract

Ca2+ transients in myocardial cells are modulated by cyclic AMP-dependent phosphorylation of a protein in the sarcoplasmic reticulum. This protein, termed phospholamban, serves to regulate the Ca2+ pump ATPase of this membrane, thus altering the mode of Ca2+ transients and the myocardial contractile response. Elucidating the structure of phospholamban and its intimate interaction with the Ca2+ pump ATPase should provide the basis for understanding, at the molecular level, how the cAMP system contributes to excitation-contraction coupling in muscle cells.

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Year:  1989        PMID: 2545189     DOI: 10.1002/bies.950100505

Source DB:  PubMed          Journal:  Bioessays        ISSN: 0265-9247            Impact factor:   4.345


  21 in total

1.  Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17.

Authors:  Piero Pollesello; Arto Annila
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

2.  NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.

Authors:  Jamillah Zamoon; Alessandro Mascioni; David D Thomas; Gianluigi Veglia
Journal:  Biophys J       Date:  2003-10       Impact factor: 4.033

3.  Cardiac-specific overexpression of sarcolipin inhibits sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA2a) activity and impairs cardiac function in mice.

Authors:  Michio Asahi; Kinya Otsu; Hiroyuki Nakayama; Shungo Hikoso; Toshihiro Takeda; Anthony O Gramolini; Maria G Trivieri; Gavin Y Oudit; Takashi Morita; Yoichiro Kusakari; Shuta Hirano; Kenichi Hongo; Shinichi Hirotani; Osamu Yamaguchi; Alan Peterson; Peter H Backx; Satoshi Kurihara; Masatsugu Hori; David H MacLennan
Journal:  Proc Natl Acad Sci U S A       Date:  2004-06-16       Impact factor: 11.205

4.  (1)H/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles.

Authors:  Emily E Metcalfe; Jamillah Zamoon; David D Thomas; Gianluigi Veglia
Journal:  Biophys J       Date:  2004-08       Impact factor: 4.033

5.  Using experimental information to produce a model of the transmembrane domain of the ion channel phospholamban.

Authors:  P Herzyk; R E Hubbard
Journal:  Biophys J       Date:  1998-03       Impact factor: 4.033

6.  Anti-phospholamban and protein kinase A alter the Ca2+ sensitivity and maximum velocity of Ca2+ uptake by the cardiac sarcoplasmic reticulum.

Authors:  M E Kargacin; Z Ali; G Kargacin
Journal:  Biochem J       Date:  1998-04-01       Impact factor: 3.857

7.  Protein-protein interactions in calcium transport regulation probed by saturation transfer electron paramagnetic resonance.

Authors:  Zachary M James; Jesse E McCaffrey; Kurt D Torgersen; Christine B Karim; David D Thomas
Journal:  Biophys J       Date:  2012-09-19       Impact factor: 4.033

8.  Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer.

Authors:  P Pollesello; A Annila; M Ovaska
Journal:  Biophys J       Date:  1999-04       Impact factor: 4.033

9.  The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm.

Authors:  Anne-Marie L Winther; Maike Bublitz; Jesper L Karlsen; Jesper V Møller; John B Hansen; Poul Nissen; Morten J Buch-Pedersen
Journal:  Nature       Date:  2013-03-03       Impact factor: 49.962

10.  Translation of Ser16 and Thr17 phosphorylation of phospholamban into Ca 2+-pump stimulation.

Authors:  W A Jackson; J Colyer
Journal:  Biochem J       Date:  1996-05-15       Impact factor: 3.857

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