Merlin differs from moesin in binding to F-actin and in its intra- and intermolecular interactions
Department of Cell Biology
3T3 Cells; Actins; Amino Acid Sequence; Animals; Cloning, Molecular; Conserved Sequence; Escherichia coli; Green Fluorescent Proteins; Humans; Luminescent Proteins; Membrane Proteins; Mice; *Microfilament Proteins; Molecular Sequence Data; Neoplasm Proteins; Neurofibromin 2; Proteins; Recombinant Fusion Proteins; Restriction Mapping; Sequence Alignment; Sequence Homology, Amino Acid; Transfection
Cell Biology | Life Sciences | Medicine and Health Sciences
The neurofibromatosis type 2 (NF2) tumor suppressor gene encodes merlin, a protein with homology to the cell membrane/F-actin linking proteins, moesin, ezrin and radixin. Unlike these closely related proteins, merlin lacks a C-terminal F-actin binding site detectable by actin blot overlays, and the GFP-tagged merlin C-terminal domain co-distributes with neither stress fibers nor cortical actin in NIH3T3 cells. Merlin also differs from the other three proteins in its inter- and intramolecular domain interactions, as shown by in vitro binding and yeast two-hybrid assays. As is true for ezrin, moesin and radixin, the N- and C-terminal domains of merlin type 1 bind to each other. However, full-length merlin and its N- and C-terminal domains, as well as the C-terminal domain of ezrin, interact with other full-length merlin type 1 molecules, and its C-terminal domain interacts with itself. Merlin 1 function in cells may thus depend on intra- and intermolecular interactions and their modulation, which include interactions with other members of this protein family.
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Citation: Biochem Biophys Res Commun. 1998 Jul 30;248(3):548-53. Link to article on publisher's site
Huang, L.; Ichimaru, E.; Pestonjamasp, Kersi N.; Cui, X.; Nakamura, H.; Lo, G. Y.; Lin, F. I.; Luna, Elizabeth J.; and Furthmayr, H., "Merlin differs from moesin in binding to F-actin and in its intra- and intermolecular interactions" (1998). Women’s Health Research Faculty Publications. 297.