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Vol. 12, Issue 4, 891-900, April 2001
and
*Howard Hughes Medical Institute, Center for Cancer
Research, Massachusetts Institute of Technology, Cambridge,
Massachusetts 02139; and The actin cytoskeleton plays a significant role in changes of cell
shape and motility, and interactions between the actin filaments and
the cell membrane are crucial for a variety of cellular processes.
Several adaptor proteins, including talin, maintain the
cytoskeleton-membrane linkage by binding to integral membrane proteins
and to the cytoskeleton. Layilin, a recently characterized transmembrane protein with homology to C-type lectins, is a
membrane-binding site for talin in peripheral ruffles of spreading
cells. To facilitate studies of layilin's function, we have generated
a layilin-Fc fusion protein comprising the extracellular part of
layilin joined to human immunoglobulin G heavy chain and used this
chimera to identify layilin ligands. Here, we demonstrate that
layilin-Fc fusion protein binds to hyaluronan immobilized to Sepharose.
Microtiter plate-binding assays, coprecipitation experiments, and
staining of sections predigested with different
glycosaminoglycan-degrading enzymes and cell adhesion assays all
revealed that layilin binds specifically to hyaluronan but not to other
tested glycosaminoglycans. Layilin's ability to bind hyaluronan, a
ubiquitous extracellular matrix component, reveals an interesting
parallel between layilin and CD44, because both can bind to
cytoskeleton-membrane linker proteins through their cytoplasmic domains
and to hyaluronan through their extracellular domains. This parallelism
suggests a role for layilin in cell adhesion and motility.
Division of Rheumatology,
Immunology and Allergy, Department of Medicine, Brigham and Women's
Hospital and Harvard Medical School, Boston, Massachusetts 02115
Present address: Department of Medical
Biochemistry and Microbiology, Uppsala University, Box 582, SE-75123
Uppsala, Sweden.
§
Corresponding author. E-mail: rohynes{at}mit.edu.
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