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Structural basis fo...
Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A
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- Löw, Christian (författare)
- Karolinska Institutet
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- Quistgaard, Esben M. (författare)
- Karolinska Institutet
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- Kovermann, Michael (författare)
- Martin-Luther-Universität Halle-Wittenberg, Germany
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- Anandapadmanaban, Madhanagopal (författare)
- Linköpings universitet,Kemi,Tekniska högskolan,Karolinska Institutet, Stockholm, Sweden
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- Balbach, Jochen (författare)
- Martin-Luther-Universität Halle-Wittenberg, Germany
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- Nordlund, Pär (författare)
- Karolinska Institutet
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(creator_code:org_t)
- 2014-07-08
- 2014
- Engelska.
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Ingår i: Biological chemistry (Print). - : Walter de Gruyter. - 1431-6730 .- 1437-4315. ; 395:7-8, s. 881-889
- Relaterad länk:
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https://dr.ntu.edu.s...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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http://kipublication...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- activation chaperone; phosphatase; posttranslational modification; signaling; X-ray structure
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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