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Cover Caption: Organization of Actin Filaments
Publication year - 2013
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/jipb.12042
Subject(s) - actin , actin binding protein , actin remodeling , cytoskeleton , actin cytoskeleton , microbiology and biotechnology , mdia1 , microfilament , cover (algebra) , chemistry , helix (gastropod) , biophysics , biology , biochemistry , cell , ecology , engineering , mechanical engineering , snail
Plant actin depolymerizing factor (ADF) binds to both monomeric and filamentous actin, and plays a key role in the organization of the actin cytoskeleton. In this issue, Dong et al. (pp. 250–261) demonstrate that charged residues Arg98 and Lys100 of ADF1 are essential for both G‐ and F‐actin binding, and that basic residues on β‐strand 5 (K82/A) and α‐helix 4 (R135/A, R137/A) form another actin binding site for F‐actin.