A Superfamily of Actin-Binding Proteins at the Actin-Membrane Nexus of Higher Plants

Michael Deeks, Joanna Calcutt, Elizabeth Ingle, Timothy Hawkins, Sean Chapman, Christine Richardson, Martin Dixon, Frances Cartwright, Andrei Smertenko, Karl Oparka, Patrick Hussey

Research output: Contribution to journalArticlepeer-review


Complex animals use a wide variety of adaptor proteins to produce specialized sites of interaction between actin and membranes. Plants do not have these protein families, yet actin-membrane interactions within plant cells are critical for the positioning of subcellular compartments, for coordinating intercellular communication, and for membrane deformation [1]. Novel factors are therefore likely to provide interfaces at actin-membrane contacts in plants, but their identity has remained obscure. Here we identify the plant-specific Networked (NET) superfamily of actin-binding proteins, members of which localize to the actin cytoskeleton and specify different membrane compartments. The founding member of the NET superfamily, NET1A, is anchored at the plasma membrane and predominates at cell junctions, the plasmodesmata. NET1A binds directly to actin filaments via a novel actin-binding domain that defines a superfamily of thirteen Arabidopsis proteins divided into four distinct phylogenetic clades. Members of other clades identify interactions at the tonoplast, nuclear membrane, and pollen tube plasma membrane, emphasizing the role of this superfamily in mediating actin-membrane interactions.
Original languageEnglish
Pages (from-to)1595–1600
JournalCurrent Biology
Issue number17
Early online date26 Jul 2012
Publication statusPublished - 2012


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