Literature DB >> 28646126

How a helix imposes palmitoylation of a membrane protein: What one can learn from NCX.

Daniel Khananshvili1.   

Abstract

Palmitoylation is a critical post-translational modification that anchors proteins to, and regulates transport across, the lipid bilayer. Palmitoylation enzymes have been assumed to select their substrates based on a protein's primary sequence, but a consensus sequence has been slow to emerge. A study of the sodium/calcium exchanger now suggests that secondary structure may hold the key to understanding the determinants of this modification.
© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

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Year:  2017        PMID: 28646126      PMCID: PMC5481581          DOI: 10.1074/jbc.H116.773945

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  10 in total

Review 1.  Sodium-calcium exchange: a molecular perspective.

Authors:  K D Philipson; D A Nicoll
Journal:  Annu Rev Physiol       Date:  2000       Impact factor: 19.318

2.  Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger.

Authors:  Jun Liao; Hua Li; Weizhong Zeng; David B Sauer; Ricardo Belmares; Youxing Jiang
Journal:  Science       Date:  2012-02-10       Impact factor: 47.728

3.  The palmitoylation machinery is a spatially organizing system for peripheral membrane proteins.

Authors:  Oliver Rocks; Marc Gerauer; Nachiket Vartak; Sebastian Koch; Zhi-Ping Huang; Markos Pechlivanis; Jürgen Kuhlmann; Lucas Brunsveld; Anchal Chandra; Bernhard Ellinger; Herbert Waldmann; Philippe I H Bastiaens
Journal:  Cell       Date:  2010-04-22       Impact factor: 41.582

4.  The crystal structure of the primary Ca2+ sensor of the Na+/Ca2+ exchanger reveals a novel Ca2+ binding motif.

Authors:  Debora A Nicoll; Michael R Sawaya; Seunghyug Kwon; Duilio Cascio; Kenneth D Philipson; Jeff Abramson
Journal:  J Biol Chem       Date:  2006-06-14       Impact factor: 5.157

5.  Ca2+ regulation in the Na+/Ca2+ exchanger involves two markedly different Ca2+ sensors.

Authors:  Mark Hilge; Jan Aelen; Geerten W Vuister
Journal:  Mol Cell       Date:  2006-04-07       Impact factor: 17.970

6.  The second Ca2+-binding domain of the Na+ Ca2+ exchanger is essential for regulation: crystal structures and mutational analysis.

Authors:  Gabriel Mercado Besserer; Michela Ottolia; Debora A Nicoll; Vincent Chaptal; Duilio Cascio; Kenneth D Philipson; Jeff Abramson
Journal:  Proc Natl Acad Sci U S A       Date:  2007-10-25       Impact factor: 11.205

7.  A common Ca2+-driven interdomain module governs eukaryotic NCX regulation.

Authors:  Moshe Giladi; Yehezkel Sasson; Xianyang Fang; Reuben Hiller; Tal Buki; Yun-Xing Wang; Joel A Hirsch; Daniel Khananshvili
Journal:  PLoS One       Date:  2012-06-29       Impact factor: 3.240

Review 8.  Structural Features of Ion Transport and Allosteric Regulation in Sodium-Calcium Exchanger (NCX) Proteins.

Authors:  Moshe Giladi; Inbal Tal; Daniel Khananshvili
Journal:  Front Physiol       Date:  2016-02-09       Impact factor: 4.566

9.  Structure-based dynamic arrays in regulatory domains of sodium-calcium exchanger (NCX) isoforms.

Authors:  Moshe Giladi; Su Youn Lee; Yarden Ariely; Yotam Teldan; Rotem Granit; Roi Strulovich; Yoni Haitin; Ka Young Chung; Daniel Khananshvili
Journal:  Sci Rep       Date:  2017-04-20       Impact factor: 4.379

10.  An amphipathic α-helix directs palmitoylation of the large intracellular loop of the sodium/calcium exchanger.

Authors:  Fiona Plain; Samitha Dilini Congreve; Rachel Sue Zhen Yee; Jennifer Kennedy; Jacqueline Howie; Chien-Wen Kuo; Niall J Fraser; William Fuller
Journal:  J Biol Chem       Date:  2017-04-21       Impact factor: 5.157

  10 in total
  1 in total

1.  Proton-modulated interactions of ions with transport sites of prokaryotic and eukaryotic NCX prototypes.

Authors:  Bosmat Refaeli; Stephanie Liu; Reuben Hiller; Moshe Giladi; Carlos R Baiz; Daniel Khananshvili
Journal:  Cell Calcium       Date:  2021-09-20       Impact factor: 6.817

  1 in total

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