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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 388, Issue 10 (Oct 2007)

Issues

An essential role for Pin1 in Xenopus laevis embryonic development revealed by specific inhibitors

Dirk Wildemann
  • 1Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
    Authors 1 and 2 contributed equally to this work.
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/ Birte Hernandez Alvarez
  • 2Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany and present address: Max Planck Institute for Developmental Biology, Department Protein Evolution, Spemannstrasse 35, D-72076 Tübingen, Germany.
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/ Gerlind Stoller
  • 3Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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/ Xiao Zhen Zhou
  • 4Cancer Biology Program, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA
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/ Kun Ping Lu
  • 5Cancer Biology Program, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA
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/ Frank Erdmann
  • 6Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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/ David Ferrari
  • 7Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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/ Gunter Fischer
  • 8Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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Published Online: 2007-10-16 | DOI: https://doi.org/10.1515/BC.2007.127

Abstract

The peptidyl prolyl cis/trans isomerase (PPIase) Pin1 plays an important role in phosphorylation-dependent events of the cell cycle. This function is linked to its display of two phosphothreonine/phosphoserine-proline binding motifs, one within the type IV WW domain and a second within the parvulin-like catalytic domain. By microinjection of the compound Ac-Phe-D-Thr(PO3H2)-Pip-Nal-Gln-NH2, which inhibits Xenopus laevis Pin1 with a K i value of 19.4±1.5 nM, into the animal pole of X. laevis embryos at the two-cell stage, the impact of Pin1 PPIase activity on cell cycle progression and embryonic development could be analysed, independent of WW domain-mediated phosphoprotein binding. Injected embryos showed a dramatically decreased survival rate at late stages of development that could only be partially compensated by co-injection with mRNAs of enzymatically active Pin1 variants, demonstrating that the phosphorylation-specific PPIase activity of Pin1 is essential for cell division and development in X. laevis.

Keywords: embryonic development; inhibition; microinjection; peptidyl prolyl cis/trans isomerase (PPIase); phosphopeptide

About the article

Corresponding author


Received: 2007-03-14

Accepted: 2007-06-25

Published Online: 2007-10-16

Published in Print: 2007-10-01


Citation Information: Biological Chemistry, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2007.127.

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