View Item 
      •   Home
      • 1. Schools
      • College of Science
      • School of Biological Sciences (SBS)
      • SBS Journal Articles
      • View Item
      •   Home
      • 1. Schools
      • College of Science
      • School of Biological Sciences (SBS)
      • SBS Journal Articles
      • View Item
      JavaScript is disabled for your browser. Some features of this site may not work without it.
      Subject Lookup

      Browse

      All of DR-NTUCommunities & CollectionsTitlesAuthorsBy DateSubjectsThis CollectionTitlesAuthorsBy DateSubjects

      My Account

      Login

      Statistics

      Most Popular ItemsStatistics by CountryMost Popular Authors

      About DR-NTU

      Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A

      Thumbnail
      Structural basis for PTPA interaction with the.pdf (1.988Mb)
      Author
      Löw, Christian
      Quistgaard, Esben M.
      Kovermann, Michael
      Anandapadamanaban, Madhanagopal
      Balbach, Jochen
      Nordlund, Pär
      Date of Issue
      2014
      School
      School of Biological Sciences
      Version
      Published version
      Abstract
      Protein phosphatase 2A (PP2A) is a highly abundant heterotrimeric Ser/Thr phosphatase involved in the regulation of a variety of signaling pathways. The PP2A phosphatase activator (PTPA) is an ATP-dependent activation chaperone, which plays a key role in the biogenesis of active PP2A. The C-terminal tail of the catalytic subunit of PP2A is highly conserved and can undergo a number of posttranslational modifications that serve to regulate the function of PP2A. Here we have studied structurally the interaction of PTPA with the conserved C-terminal tail of the catalytic subunit carrying different posttranslational modifications. We have identified an additional interaction site for the invariant C-terminal tail of the catalytic subunit on PTPA, which can be modulated via posttranslational modifications. We show that phosphorylation of Tyr307PP2A-C or carboxymethylation of Leu309PP2A-C abrogates or diminishes binding of the C-terminal tail, whereas phosphorylation of Thr304PP2A-C is of no consequence. We suggest that the invariant C-terminal residues of the catalytic subunit can act as affinity enhancer for different PP2A interaction partners, including PTPA, and a different ‘code’ of posttranslational modifications can favour interactions to one subunit over others.
      Subject
      DRNTU::Science::Biological sciences::Biochemistry
      Type
      Journal Article
      Series/Journal Title
      Biological chemistry
      Rights
      © 2014 De Gruyter. This paper was published in Biological Chemistry and is made available as an electronic reprint (preprint) with permission of De Gruyter. The paper can be found at the following official DOI: [http://dx.doi.org/10.1515/hsz-2014-0106].  One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
      Collections
      • SBS Journal Articles
      http://dx.doi.org/10.1515/hsz-2014-0106
      Get published version (via Digital Object Identifier)

      Show full item record


      NTU Library, Nanyang Avenue, Singapore 639798 © 2011 Nanyang Technological University. All rights reserved.
      DSpace software copyright © 2002-2015  DuraSpace
      Contact Us | Send Feedback
      Share |    
      Theme by 
      Atmire NV
       

       


      NTU Library, Nanyang Avenue, Singapore 639798 © 2011 Nanyang Technological University. All rights reserved.
      DSpace software copyright © 2002-2015  DuraSpace
      Contact Us | Send Feedback
      Share |    
      Theme by 
      Atmire NV
       

       

      DCSIMG