Jump to ContentJump to Main Navigation
Show Summary Details
In This Section

Thomas, Douglas D.

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751

Online
ISSN
1437-4315
See all formats and pricing
In This Section
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.
/ 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.
/ Gerlind Stoller
  • 3Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
/ Xiao Zhen Zhou
  • 4Cancer Biology Program, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA
/ Kun Ping Lu
  • 5Cancer Biology Program, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA
/ Frank Erdmann
  • 6Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
/ David Ferrari
  • 7Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
/ Gunter Fischer
  • 8Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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. Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Tae Ho Lee, Lucia Pastorino, and Kun Ping Lu
Expert Reviews in Molecular Medicine, 2011, Volume 13

Comments (0)

Please log in or register to comment.
Log in