Layilin, a cell surface hyaluronan receptor, interacts with merlin and radixin

Journal Article · Mon Aug 01 04:00:00 EDT 2005 · Experimental Cell Research

DOI:https://doi.org/10.1016/j.yexcr.2005.04.017· OSTI ID:20717638

Bono, Petri ^[1]; Cordero, Etchell ^[1]; Johnson, Kristen ^[1]; Borowsky, Mark ^[1]; Ramesh, Vijaya ^[2]; Jacks, Tyler ^[1]; Hynes, Richard O ^[1]

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1. Howard Hughes Medical Institute, Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139 (United States)
2. Molecular Neurogenetics Unit, Massachusetts General Hospital, Charlestown, MA 02129 (United States)

Layilin is a widely expressed integral membrane hyaluronan receptor, originally identified as a binding partner of talin located in membrane ruffles. We have identified merlin, the neurofibromatosis type 2 tumor suppressor protein and radixin, as other interactors with the carboxy-terminal domain of layilin. We show that the carboxy-terminal domain of layilin is capable of binding to the amino-terminal domain of radixin. An interdomain interaction between the amino- and the carboxy-terminal domains of radixin inhibits its ability to bind to layilin. In the presence of acidic phospholipids, the interdomain interaction of radixin is inhibited and layilin can bind to full-length radixin. In contrast, layilin binds both full-length and amino-terminal merlin-GST fusion proteins without a requirement for phospholipids. Furthermore, layilin antibody can immunoprecipitate merlin, confirming association in vivo between these two proteins, which also display similar subcellular localizations in ruffling membranes. No interaction was observed between layilin and ezrin or layilin and moesin. These findings expand the known binding partners of layilin to include other members of the talin/band 4.1/ERM (ezrin, radixin, and moesin) family of cytoskeletal-membrane linker molecules. This in turn suggests that layilin may mediate signals from extracellular matrix to the cell cytoskeleton via interaction with different intracellular binding partners and thereby be involved in the modulation of cortical structures in the cell.

• OSTI ID: 20717638
• Journal Information: Experimental Cell Research, Journal Name: Experimental Cell Research Journal Issue: 1 Vol. 308; ISSN 0014-4827; ISSN ECREAL
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ANTIBODIES
CHOLINE
GLUTATHIONE
IMMUNOGLOBULINS
IN VIVO
MICROTUBULES
NEOPLASMS
PEROXIDASES
PHOSPHATES
PHOSPHOLIPIDS
RECEPTORS
SALTS
SODIUM