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Titolo:
The neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral association
Autore:
James, MF; Manchanda, N; Gonzalez-Agosti, C; Hartwig, JH; Ramesh, V;
Indirizzi:
Massachusetts Gen Hosp, Mol Neurogenet Unit, Charlestown, MA 02129 USA Massachusetts Gen Hosp Charlestown MA USA 02129 Charlestown, MA 02129 USA Brigham & Womens Hosp, Longwood Med Res Ctr, Div Expt Med, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 Expt Med, Boston, MA 02115 USA
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 356, anno: 2001,
parte:, 2
pagine: 377 - 385
SICI:
0264-6021(20010601)356:<377:TN2PPM>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXCHANGER REGULATORY FACTOR; TRANSMEMBRANE CONDUCTANCE REGULATOR; CELL EXTENSION ACTIVITY; NHE-RF; EZRIN/RADIXIN/MOESIN PROTEINS; BETA(2)-ADRENERGIC RECEPTOR; CAPPING PROTEIN; TERMINAL DOMAIN; ERM PROTEINS; EZRIN;
Keywords:
actin cytoskeleton; ezrin/radixin/moesin family; merlin; neurofibromatosis 2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Ramesh, V Massachusetts Gen Hosp, Mol Neurogenet Unit, Bldg 149,13th St, Charlestown, MA 02129 USA Massachusetts Gen Hosp Bldg 149,13th St Charlestown MA USA 02129
Citazione:
M.F. James et al., "The neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral association", BIOCHEM J, 356, 2001, pp. 377-385

Abstract

The neurofibromatosis 2 protein product merlin, named for its relatedness to the ezrin, radixin and moesin (ERM) family of proteins, is a tumour suppressor whose absence results in the occurrence of multiple tumours of the nervous system, particularly schwannomas and meningiomas. Merlin's similarity to ERMs suggests that it might share functions, acting as a link between cytoskeletal components and the cell membrane. The N-terminus of merlin hasstrong sequence identity to the N-terminal actin-binding region of ezrin; here we describe in detail the merlin-actin interaction. Employing standardactin co-sedimentation assays, we have determined that merlin isoform 2 binds F-actin with an apparent binding constant of 3.6 muM and a stoichiometry of 1 mol of merlin per 11.5 mol of actin in filaments at saturation. Further, solid-phase binding assays reveal that merlin isoforms 1 and 2 bind actin filaments differentially, suggesting that the intramolecular interactions in isoform 1 might hinder its ability to bind actin. However, merlin does not bind G-actin. Studies of actin filament dynamics show that merlin slows filament disassembly with no influence on the assembly rate, indicating that merlin binds along actin filament lengths. This conclusion is supported by electron microscopy, which demonstrates that merlin binds periodicallyalong cytoskeletal actin filaments. Comparison of these findings with those reported for ERM proteins reveal a distinct role for merlin in actin filament dynamics.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 00:01:57