Skip to main content
construction release_alert
Scholars@Duke will be undergoing maintenance April 11-15. Some features may be unavailable during this time.
cancel

Cyclin-binding motifs are essential for the function of p21CIP1.

Publication ,  Journal Article
Chen, J; Saha, P; Kornbluth, S; Dynlacht, BD; Dutta, A
Published in: Molecular and cellular biology
September 1996

The cyclin-dependent kinase (Cdk) inhibitor p21 is induced by the tumor suppressor p53 and is required for the G1-S block in cells with DNA damage. We report that there are two copies of a cyclin-binding motif in p21, Cy1 and Cy2, which interact with the cyclins independently of Cdk2. The cyclin-binding motifs of p21 are required for optimum inhibition of cyclin-Cdk kinases in vitro and for growth suppression in vivo. Peptides containing only the Cy1 or Cy2 motif partially inhibit cyclin-Cdk kinase activity in vitro and DNA replication in Xenopus egg extracts. A monoclonal antibody which recognizes the Cy1 site of p21 specifically disrupts the association of p21 with cyclin E-Cdk2 and with cyclin D1-Cdk4 in cell extracts. Taken together, these observations suggest that the cyclin-binding motif of p21 is important for kinase inhibition and for formation of p21-cyclin-Cdk complexes in the cell. Finally, we show that the cyclin-Cdk complex is partially active if associated with only the cyclin-binding motif of p21, providing an explanation for how p21 is found associated with active cyclin-Cdk complexes in vivo. The Cy sequences may be general motifs used by Cdk inhibitors or substrates to interact with the cyclin in a cyclin-Cdk complex.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Molecular and cellular biology

DOI

EISSN

1098-5549

ISSN

0270-7306

Publication Date

September 1996

Volume

16

Issue

9

Start / End Page

4673 / 4682

Related Subject Headings

  • Xenopus laevis
  • Xenopus Proteins
  • Structure-Activity Relationship
  • Recombinant Fusion Proteins
  • Protein Serine-Threonine Kinases
  • Protein Conformation
  • Protein Binding
  • Peptide Fragments
  • Molecular Sequence Data
  • Escherichia coli
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Chen, J., Saha, P., Kornbluth, S., Dynlacht, B. D., & Dutta, A. (1996). Cyclin-binding motifs are essential for the function of p21CIP1. Molecular and Cellular Biology, 16(9), 4673–4682. https://doi.org/10.1128/mcb.16.9.4673
Chen, J., P. Saha, S. Kornbluth, B. D. Dynlacht, and A. Dutta. “Cyclin-binding motifs are essential for the function of p21CIP1.Molecular and Cellular Biology 16, no. 9 (September 1996): 4673–82. https://doi.org/10.1128/mcb.16.9.4673.
Chen J, Saha P, Kornbluth S, Dynlacht BD, Dutta A. Cyclin-binding motifs are essential for the function of p21CIP1. Molecular and cellular biology. 1996 Sep;16(9):4673–82.
Chen, J., et al. “Cyclin-binding motifs are essential for the function of p21CIP1.Molecular and Cellular Biology, vol. 16, no. 9, Sept. 1996, pp. 4673–82. Epmc, doi:10.1128/mcb.16.9.4673.
Chen J, Saha P, Kornbluth S, Dynlacht BD, Dutta A. Cyclin-binding motifs are essential for the function of p21CIP1. Molecular and cellular biology. 1996 Sep;16(9):4673–4682.

Published In

Molecular and cellular biology

DOI

EISSN

1098-5549

ISSN

0270-7306

Publication Date

September 1996

Volume

16

Issue

9

Start / End Page

4673 / 4682

Related Subject Headings

  • Xenopus laevis
  • Xenopus Proteins
  • Structure-Activity Relationship
  • Recombinant Fusion Proteins
  • Protein Serine-Threonine Kinases
  • Protein Conformation
  • Protein Binding
  • Peptide Fragments
  • Molecular Sequence Data
  • Escherichia coli