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Direct interaction of actin filaments with F ‐ BAR protein pacsin2
Author(s) -
Kostan Julius,
Salzer Ulrich,
Orlova Albina,
Törö Imre,
Hodnik Vesna,
Senju Yosuke,
Zou Juan,
Schreiner Claudia,
Steiner Julia,
Meriläinen Jari,
Nikki Marko,
Virtanen Ismo,
Carugo Oliviero,
Rappsilber Juri,
Lappalainen Pekka,
Lehto VeliPekka,
Anderluh Gregor,
Egelman Edward H,
DjinovićCarugo Kristina
Publication year - 2014
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201439267
Subject(s) - actin , cytoskeleton , microbiology and biotechnology , actin cytoskeleton , membrane , chemistry , actin remodeling , biophysics , biology , biochemistry , cell
Two mechanisms have emerged as major regulators of membrane shape: BAR domain‐containing proteins, which induce invaginations and protrusions, and nuclear promoting factors, which cause generation of branched actin filaments that exert mechanical forces on membranes. While a large body of information exists on interactions of BAR proteins with membranes and regulatory proteins of the cytoskeleton, little is known about connections between these two processes. Here, we show that the F‐ BAR domain protein pacsin2 is able to associate with actin filaments using the same concave surface employed to bind to membranes, while some other tested N‐ BAR and F‐ BAR proteins (endophilin, CIP 4 and FCHO 2) do not associate with actin. This finding reveals a new level of complexity in membrane remodeling processes.