Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A
2014 (English)In: Biological chemistry (Print), ISSN 1431-6730, E-ISSN 1437-4315, Vol. 395, no 7-8, 881-889 p.Article in journal (Refereed) Published
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 Tyr307(PP2A-C) or carboxymethylation of Leu309(PP2A-C) abrogates or diminishes binding of the C-terminal tail, whereas phosphorylation of Thr304(PP2A-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.
Place, publisher, year, edition, pages
Walter de Gruyter, 2014. Vol. 395, no 7-8, 881-889 p.
activation chaperone; phosphatase; posttranslational modification; signaling; X-ray structure
IdentifiersURN: urn:nbn:se:liu:diva-109228DOI: 10.1515/hsz-2014-0106ISI: 000338844300017PubMedID: 25003389OAI: oai:DiVA.org:liu-109228DiVA: diva2:737196