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Cingulin interacts with F‐actin in vitro
Author(s) -
D'Atri Fabio,
Citi Sandra
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02936-2
Subject(s) - actin , xenopus , in vitro , cytoplasm , microbiology and biotechnology , biology , actin binding protein , chemistry , cytoskeleton , actin cytoskeleton , biochemistry , gene , cell
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.