Scopus Publication Detail
The publication detail shows the title, authors (with indicators showing other profiled authors), information on the publishing organization, abstract and a link to the article in Scopus. This abstract is what is used to create the fingerprint of the publication.
Role of leucine 31 of phospholamban in structural and functional interactions with the ca2+ pump of cardiac sarcoplasmic reticulum
Journal of Biological Chemistry. 2005;280(11):10530-10539.Abstract
The ability of two loss-of-function mutants, L31A and L31C, of phospholamban (PLB) to bind to and inhibit the Ca2+ pump of cardiac sarcoplasmic reticulum (SERCA2a) was investigated using a molecular cross-linking approach. Leu31 of PLB, located at the cytoplasmic membrane boundary, is a critical amino acid shown previously to be essential for Ca2+-ATPase inhibition. We observed that L31A or L31C mutations of PLB prevented the inhibition of Ca2+-ATPase activity and disabled the cross-linking of N27C and N30C of PLB to Lys328 and Cys 318 of SERCA2a. Although L31C-PLB failed to cross-link to any Cys or Lys residue of wild-type SERCA2a, L31C did cross-link with high efficiency to T317C of SERCA2a with use of the homobifunctional sulfhydryl cross-linking reagent, 1,6-bismaleimidohexane. This places Leu31 of PLB within 10 Å of Thr317 of SERCA2a in the M4 helix. Thus, contrary to previous suggestions, PLB with loss-of-function mutations at Leu31 retains the ability to bind to SERCA2a, despite losing inhibitory activity. Cross-linking of L31C-PLB to T317C-SERCA2a occurred only in the absence of Ca2+ and in the presence of nucleotide and was prevented by thapsigargin and by anti-PLB antibody, demonstrating for a fourth cross-linking pair that PLB interacts near M4 only when the Ca2+ pump is in the Ca2+-free, nucleotide-bound E2 conformation, but not in the E2 state inhibited by thapsigargin. L31I-PLB retained full functional and cross-linking activity, suggesting that a bulky hydrophobic residue at position 31 of PLB is essential for productive interaction with SERCA2a. A model for the three-dimensional structure of the interaction site is proposed. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
This section shows information related to the publication - computed using the fingerprint of the publication - including related publications, related experts with fingerprints representing significant amounts of overlap between their fingerprint and this publication. The red dots indicate whether those experts or terms appear within the publication, thereby showing potential and actual connections.
Zhenhui Chen; David L. Stokes; William J. Rice; Larry R. JonesJournal of Biological Chemistry. 2003;278(48):48348-48356.
Zhenhui Chen; Brandy L. Akin; David L. Stokes; Larry R. JonesJournal of Biological Chemistry. 2006;281(20):14163-14172.
Zhenhui Chen; Brandy L. Akin; Larry R. JonesJournal of Biological Chemistry. 2010;285(5):3253-3260.
Appears in this Document