In plants, the cortical endoplasmic reticulum (ER) network is connected to the plasma membrane (PM) through the ER-PM contact sites (EPCSs), whose structures are maintained by EPCS resident proteins and the cytoskeleton. Strong co-alignment between EPCSs and the cytoskeleton is observed in plants, but little is known of how the cytoskeleton is maintained and regulated at the EPCS. Here, we have used a yeast-two-hybrid screen and subsequent in vivo interaction studies in plants by fluorescence resonance energy transfer (FRET)-fluorescence lifetime imaging microscopy (FLIM) analysis to identify two microtubule binding proteins, KLCR1 (kinesin-light-chain-related protein 1) and IQD2 (IQ67-domain 2), that interact with the actin binding protein NET3C and form a component of plant EPCS that mediates the link between the actin and microtubule networks. The NET3C-KLCR1-IQD2 module, acting as an actin-microtubule bridging complex, has a direct influence on ER morphology and EPCS structure. Their loss-of-function mutants, net3a/NET3C RNAi, klcr1, or iqd2, exhibit defects in pavement cell morphology, which we suggest is linked to the disorganization of both actin filaments and microtubules. In conclusion, our results reveal a novel cytoskeletal-associated complex, which is essential for the maintenance and organization of cytoskeletal structure and ER morphology at the EPCS and for normal plant cell morphogenesis.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.cub.2020.12.009 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Coupling of dynamic microtubules to F-actin by Fmn2 regulates chemotaxis of neuronal growth cones.
J Cell Sci
July 2021
Indian Institute of Science Education and Research (IISER) Pune, Dr Homi Bhabha Road, Pune 411008, India.
Dynamic co-regulation of the actin and microtubule subsystems enables the highly precise and adaptive remodelling of the cytoskeleton necessary for critical cellular processes, such as axonal pathfinding. The modes and mediators of this interpolymer crosstalk, however, are inadequately understood. We identify Fmn2, a non-diaphanous-related formin associated with cognitive disabilities, as a novel regulator of cooperative actin-microtubule remodelling in growth cones of both chick and zebrafish neurons.
View Article and Find Full Text PDFA novel plant actin-microtubule bridging complex regulates cytoskeletal and ER structure at ER-PM contact sites.
Curr Biol
March 2021
Key Laboratory of Horticultural Plant Biology (MOE), College of Horticulture and Forestry Sciences, Huazhong Agricultural University, Wuhan 430070, Hubei Province, China; Interdisciplinary Sciences Research Institute, Huazhong Agricultural University, Wuhan 430007, China. Electronic address:
In plants, the cortical endoplasmic reticulum (ER) network is connected to the plasma membrane (PM) through the ER-PM contact sites (EPCSs), whose structures are maintained by EPCS resident proteins and the cytoskeleton. Strong co-alignment between EPCSs and the cytoskeleton is observed in plants, but little is known of how the cytoskeleton is maintained and regulated at the EPCS. Here, we have used a yeast-two-hybrid screen and subsequent in vivo interaction studies in plants by fluorescence resonance energy transfer (FRET)-fluorescence lifetime imaging microscopy (FLIM) analysis to identify two microtubule binding proteins, KLCR1 (kinesin-light-chain-related protein 1) and IQD2 (IQ67-domain 2), that interact with the actin binding protein NET3C and form a component of plant EPCS that mediates the link between the actin and microtubule networks.
View Article and Find Full Text PDFActin, microtubule, septin and ESCRT filament remodeling during late steps of cytokinesis.
Curr Opin Cell Biol
February 2018
Membrane Traffic and Cell Division Lab, Cell Biology and Infection Department, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris cedex 15, France; Centre National de la Recherche Scientifique CNRS UMR3691, 75015 Paris, France. Electronic address:
Cytokinesis is the process by which a mother cell is physically cleaved into two daughter cells. In animal cells, cytokinesis begins with the contraction of a plasma membrane-associated actomyosin ring that is responsible for the ingression of a cleavage furrow. However, the post-furrowing steps of cytokinesis are less understood.
View Article and Find Full Text PDFMicrotubule-associated proteins as direct crosslinkers of actin filaments and microtubules.
IUBMB Life
June 2015
Transmission Electron Microscope Laboratory, Biomedical Technology Wing, Sree Chitra Tirunal Institute for Medical Sciences and Technology, Thiruvananthapuram, Kerala, India.
The cytoskeletal polymers--actin, microtubules, and intermediate filaments--are interlinked by coordinated protein interactions to form a complex three-dimensional cytoskeletal network. Association of actin filaments with microtubules is important for various cellular processes such as cell division, migration, vesicle and organelle transport, and axonal growth. Several proteins including signaling molecules, motor proteins, and proteins directly or indirectly associated with microtubules and actin are involved in bridging the cytoskeletal components.
View Article and Find Full Text PDFThe actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition.
Mol Biol Cell
September 2013
Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280 Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280 Carolina Center for Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280 Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Actin and microtubule dynamics must be precisely coordinated during cell migration, mitosis, and morphogenesis--much of this coordination is mediated by proteins that physically bridge the two cytoskeletal networks. We have investigated the regulation of the Drosophila actin-microtubule cross-linker Short stop (Shot), a member of the spectraplakin family. Our data suggest that Shot's cytoskeletal cross-linking activity is regulated by an intramolecular inhibitory mechanism.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!