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Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B

Author

Listed:
  • Holger Rehmann

    (Centre for Biomedical Genetics and Cancer Genomics Centre, University Medical Center, Universiteitsweg 100)

  • Ernesto Arias-Palomo

    (Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain)

  • Michael A. Hadders

    (Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands)

  • Frank Schwede

    (BIOLOG Life Science Institute, Flughafendamm 9a, 28199 Bremen, Germany)

  • Oscar Llorca

    (Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain)

  • Johannes L. Bos

    (Centre for Biomedical Genetics and Cancer Genomics Centre, University Medical Center, Universiteitsweg 100)

Abstract

Epac proteins: changes on cyclic AMP binding Epac proteins are activated by binding of cyclic AMP (cAMP) and act as guanine nucleotide exchange factors for Rap GTPases. They are important in the regulation of cell adhesion and insulin secretion. Here, the structure of Epac2 in a complex with cAMP and Rap1B is determined. Comparison of this activated state of the complex with the inactive one reveals the conformational changes in Epac2 induced by cAMP binding.

Suggested Citation

  • Holger Rehmann & Ernesto Arias-Palomo & Michael A. Hadders & Frank Schwede & Oscar Llorca & Johannes L. Bos, 2008. "Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B," Nature, Nature, vol. 455(7209), pages 124-127, September.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7209:d:10.1038_nature07187
    DOI: 10.1038/nature07187
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    Cited by:

    1. Candice Sartre & François Peurois & Marie Ley & Marie-Hélène Kryszke & Wenhua Zhang & Delphine Courilleau & Rodolphe Fischmeister & Yves Ambroise & Mahel Zeghouf & Sarah Cianferani & Yann Ferrandez & , 2023. "Membranes prime the RapGEF EPAC1 to transduce cAMP signaling," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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