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Medientyp:
E-Artikel
Titel:
RefilinB (FAM101B) targets FilaminA to organize perinuclear actin networks and regulates nuclear shape
Beteiligte:
Gay, Olivia;
Gilquin, Benoît;
Nakamura, Fumihiko;
Jenkins, Zandra A.;
McCartney, Rosannah;
Krakow, Deborah;
Deshiere, Alexandre;
Assard, Nicole;
Hartwig, John H.;
Robertson, Stephen P.;
Baudier, Jacques
Erschienen:
Proceedings of the National Academy of Sciences, 2011
Erschienen in:Proceedings of the National Academy of Sciences
Sprache:
Englisch
DOI:
10.1073/pnas.1104211108
ISSN:
0027-8424;
1091-6490
Entstehung:
Anmerkungen:
Beschreibung:
<jats:p>
The intracellular localization and shape of the nucleus plays a central role in cellular and developmental processes. In fibroblasts, nuclear movement and shape are controlled by a specific perinuclear actin network made of contractile actin filament bundles called transmembrane actin-associated nuclear (TAN) lines that form a structure called the actin cap. The identification of regulatory proteins associated with this specific actin cytoskeletal dynamic is a priority for understanding actin-based changes in nuclear shape and position in normal and pathological situations. Here, we first identify a unique family of actin regulators, the refilin proteins (RefilinA and RefilinB), that stabilize specifically perinuclear actin filament bundles. We next identify the actin-binding filamin A (FLNA) protein as the downstream effector of refilins. Refilins act as molecular switches to convert FLNA from an actin branching protein into one that bundles. In NIH 3T3 fibroblasts, the RefilinB/FLNA complex organizes the perinuclear actin filament bundles forming the actin cap. Finally, we demonstrate that in epithelial normal murine mammary gland (NmuMG) cells, the RefilinB/FLNA complex controls formation of a new perinuclear actin network that accompanies nuclear shape changes during the epithelial–mesenchymal transition (EMT). Our studies open perspectives for further functional analyses of this unique actin-based network and shed light on FLNA function during development and in human syndromes associated with
<jats:italic>FLNA</jats:italic>
mutations.
</jats:p>