Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism-Reference-Cited by-同舟云学术

Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism

Published:1997-12-12 Issue:5345 Volume:278 Page:1957-1960
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Yaffe Michael B.¹²³⁴⁵,Schutkowski Mike¹²³⁴⁵,Shen Minhui¹²³⁴⁵,Zhou Xiao Zhen¹²³⁴⁵,Stukenberg P. Todd¹²³⁴⁵,Rahfeld Jens-Ulrich¹²³⁴⁵,Xu Jian¹²³⁴⁵,Kuang Jian¹²³⁴⁵,Kirschner Marc W.¹²³⁴⁵,Fischer Gunter¹²³⁴⁵,Cantley Lewis C.¹²³⁴⁵,Lu Kun Ping¹²³⁴⁵

Affiliation:

1. M. B. Yaffe, Division of Signal Transduction, Department of Medicine and Department of Surgery, Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.

2. M. Schutkowski, J.-U. Rahfeld, G. Fischer, Max-Planck Research Unit on Enzymology of Protein Folding, Kurth-Mothes Strasse 3, 06120 Halle, Germany.

3. M. Shen and X. Z. Zhou, Cancer Biology Program, Division of Hematology and Oncology, Department of Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.

4. P. T. Stukenberg and M. W. Kirschner, Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

5. J. Xu, Division of Signal Transduction, Department of Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.

Abstract

Pin1 is an essential and conserved mitotic peptidyl-prolyl isomerase (PPIase) that is distinct from members of two other families of conventional PPIases, cyclophilins and FKBPs (FK-506 binding proteins). In response to their phosphorylation during mitosis, Pin1 binds and regulates members of a highly conserved set of proteins that overlaps with antigens recognized by the mitosis-specific monoclonal antibody MPM-2. Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Both Pin1 and MPM-2 selected similar phosphorylated serine-proline–containing peptides, providing the basis for the specific interaction between Pin1 and MPM-2 antigens. Pin1 preferentially isomerized proline residues preceded by phosphorylated serine or threonine with up to 1300-fold selectivity compared with unphosphorylated peptides. Pin1 may thus regulate mitotic progression by catalyzing sequence-specific and phosphorylation-dependent proline isomerization.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference44 articles.

1. Ordering S phase and M phase in the cell cycle

2. ; R. W. King P. K. Jackson M. W. Kirschner ibid. p. 563; T. R. Coleman and W. G. Dunphy Curr. Opin. Cell Biol. 6 877 (1994).

3. Cyclin-dependent protein kinases: Key regulators of the eukaryotic cell cycle

4. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis

5. Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2

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