Journal article
A Superfamily of Actin-Binding Proteins at the Actin-Membrane Nexus of Higher Plants
Current biology, Vol.22(17), pp.1595-1600
09/11/2012
Handle:
https://hdl.handle.net/2376/107048
PMID: 22840520
Abstract
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.
► NET1A is an actin-binding protein isolated from an in vivo fusion library screen ► NET1A associates with the plasma membrane and cell junctions, the plasmodesmata ► A common domain shared by NET proteins mediates the cytoskeletal interaction ► NET2/3/4 subfamilies have distinct clade-specific membrane associations
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Details
- Title
- A Superfamily of Actin-Binding Proteins at the Actin-Membrane Nexus of Higher Plants
- Creators
- Michael J Deeks - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKJoanna R Calcutt - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKElizabeth K.S Ingle - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKTimothy J Hawkins - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKSean Chapman - James Hutton Institute, Invergowrie, Dundee DD2 5DA, UKA. Christine Richardson - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKDavid A Mentlak - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKMartin R Dixon - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKFrances Cartwright - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKAndrei P Smertenko - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UKKarl Oparka - Institute of Molecular Plant Sciences, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UKPatrick J Hussey - School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UK
- Publication Details
- Current biology, Vol.22(17), pp.1595-1600
- Academic Unit
- Biological Chemistry, Institute of
- Publisher
- Elsevier Inc
- Number of pages
- 6
- Grant note
- Gatsby Foundation BB/G006334/1 / Biotechnology and Biological Sciences Research Council; UK Research & Innovation (UKRI); Biotechnology and Biological Sciences Research Council (BBSRC) BB/G006334/1 / BBSRC; UK Research & Innovation (UKRI); Biotechnology and Biological Sciences Research Council (BBSRC)
- Identifiers
- 99900547088201842
- Language
- English
- Resource Type
- Journal article