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© The Rockefeller University Press, 0021-9525/1998//429 $5.00
The Journal of Cell Biology, Volume 143, Number 2, , 1998 429-442

Layilin, A Novel Talin-binding Transmembrane Protein Homologous with C-type Lectins, is Localized in Membrane Ruffles

Howard Hughes Medical Institute, Center for Cancer Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Changes in cell morphology and motility are mediated by the actin cytoskeleton. Recent advances in our understanding of the regulators of microfilament structure and dynamics have shed light on how these changes are controlled, and efforts continue to define all the structural and signaling components involved in these processes. The actin cytoskeleton-associated protein talin binds to integrins, vinculin, and actin. We report a new binding partner for talin that we have named layilin, which contains homology with C-type lectins, is present in numerous cell lines and tissue extracts, and is expressed on the cell surface. Layilin colocalizes with talin in membrane ruffles, and is recruited to membrane ruffles in cells induced to migrate in in vitro wounding experiments and in peripheral ruffles in spreading cells. A ten–amino acid motif in the layilin cytoplasmic domain is sufficient for talin binding. We have identified a short region within talin's amino-terminal 435 amino acids capable of binding to layilin in vitro. This region overlaps a binding site for focal adhesion kinase.

Key Words: layilin • talin • ruffles • C-type lectin • focal adhesion kinase (FAK)

Abbreviations used in this paper: CRD, carbohydrate-recognition domains; ERM, ezrin/radixin/moesin; GST, glutathione-S-transferase; nt, nucleotide.

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