Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules.
Coronin 1 is a member of the coronin protein family specifically expressed in leukocytes and accumulates at sites of rearrangements of the F-actin cytoskeleton. Here, we describe that coronin 1 molecules are coiled coil-mediated homotrimeric complexes, which associate with the plasma membrane and with the cytoskeleton via two distinct domains. ... Association with the cytoskeleton was mediated by trimerization of a stretch of positively charged residues within a linker region between the N-terminal, WD repeat-containing domain and the C-terminal coiled coil. In contrast, neither the coiled coil nor the positively charged residues within the linker domain were required for plasma membrane binding, suggesting that the N-terminal, WD repeat-containing domain mediates membrane interaction. The capacity of coronin 1 to link the leukocyte cytoskeleton to the plasma membrane may serve to integrate outside-inside signaling with modulation of the cytoskeleton.
Mesh Terms:
Actins, Amino Acid Sequence, Animals, Cell Line, Cell Membrane, Circular Dichroism, Cytoskeleton, Electrophoresis, Gel, Two-Dimensional, Humans, Immunohistochemistry, Introns, Jurkat Cells, Leukocytes, Macrophages, Mice, Microfilament Proteins, Models, Biological, Molecular Sequence Data, Protein Isoforms, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Analysis, Protein, Sequence Homology, Amino Acid, Spectrophotometry, Ultraviolet, Subcellular Fractions
Actins, Amino Acid Sequence, Animals, Cell Line, Cell Membrane, Circular Dichroism, Cytoskeleton, Electrophoresis, Gel, Two-Dimensional, Humans, Immunohistochemistry, Introns, Jurkat Cells, Leukocytes, Macrophages, Mice, Microfilament Proteins, Models, Biological, Molecular Sequence Data, Protein Isoforms, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Analysis, Protein, Sequence Homology, Amino Acid, Spectrophotometry, Ultraviolet, Subcellular Fractions
Mol. Biol. Cell
Date: Jun. 01, 2005
PubMed ID: 15800061
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