1. Arabidopsis CROLIN1, a Novel Plant Actin-binding Protein, Functions in Cross-linking and Stabilizing Actin Filaments
- Author
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Honglei Jia, Tingting Fan, Jingen Zhu, Jisheng Li, Haiyun Ren, Jiaojiao Wang, Yun Xiang, Dong Qian, Lizhe An, and Yuelong Zhou
- Subjects
Arabidopsis Proteins ,Microfilament Proteins ,Molecular Sequence Data ,Arabidopsis ,Plant Biology ,food and beverages ,Arp2/3 complex ,Actin remodeling ,Pollen Tube ,macromolecular substances ,Cell Biology ,Biology ,Microfilament ,Biochemistry ,Actins ,Cell biology ,Profilin ,biology.protein ,Latrunculin ,Amino Acid Sequence ,Actin-binding protein ,MDia1 ,Cytoskeleton ,Molecular Biology - Abstract
Higher order actin filament structures are necessary for cytoplasmic streaming, organelle movement, and other physiological processes. However, the mechanism by which the higher order cytoskeleton is formed in plants remains unknown. In this study, we identified a novel actin-cross-linking protein family (named CROLIN) that is well conserved only in the plant kingdom. There are six isovariants of CROLIN in the Arabidopsis genome, with CROLIN1 specifically expressed in pollen. In vitro biochemical analyses showed that CROLIN1 is a novel actin-cross-linking protein with binding and stabilizing activities. Remarkably, CROLIN1 can cross-link actin bundles into actin networks. CROLIN1 loss of function induces pollen germination and pollen tube growth hypersensitive to latrunculin B. All of these results demonstrate that CROLIN1 may play an important role in stabilizing and remodeling actin filaments by binding to and cross-linking actin filaments.
- Published
- 2013
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