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Journal article

Cingulin interacts with F-actin in vitro.

  • D'Atri F Department of Molecular Biology, University of Geneva, Geneva 4, Switzerland.
  • Citi S
  • 2001-10-30
Published in:
  • FEBS letters. - 2001
Actins
Animals
Binding Sites
Cross-Linking Reagents
Cytoskeleton
Humans
In Vitro Techniques
Membrane Proteins
Microfilament Proteins
Peptide Mapping
Protein Binding
Rabbits
Recombinant Fusion Proteins
Spodoptera
Tight Junctions
Xenopus Proteins
Xenopus laevis
English Cingulin, a M(r) 140-160 kDa protein of the cytoplasmic plaque of epithelial tight junctions (TJ), interacts in vitro with TJ proteins and myosin. Here we investigated cingulin interaction with actin, using His-tagged, full-length Xenopus laevis cingulin expressed in insect cells, and glutathione S-transferase (GST) fusion proteins of fragments of cingulin expressed in bacteria. Purified full-length cingulin co-pelleted with F-actin after high speed centrifugation, and promoted the sedimentation of F-actin under low speed centrifugation, suggesting that cingulin is an actin-cross-linking protein. The actin interaction of GST fusion proteins containing fragments of Xenopus cingulin suggested that the F-actin binding site is between residues 101 and 294.
Language
  • English
Open access status
bronze
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Persistent URL
https://sonar.ch/global/documents/145710
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