Formin nanoclustering-mediated actin assembly during plant flagellin and DSF signaling

Ma, Zhiming; Liu, Xiaolin; Nath, Sangeeta; Sun, He; Tran, Tuan Minh; Yang, Liang; Mayor, Satyajit; Miao, Yansong

doi:10.1016/j.celrep.2021.108884

Cited by 36 publications

(53 citation statements)

References 107 publications

(145 reference statements)

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“…Indeed, some proteins are known to act as molecular bridges between cell wall components and actin filaments. Indeed, formins interact from one side with the cell wall, likely via their proline-rich repeat stretch in their extracellular domain, and from the other side with actin filaments via their cytoplasmic formin homology domain ( Michelot et al, 2005 ; Martinière et al, 2011 ; Ma et al, 2021 ). A recent preprint study suggests that this transmembrane connection is necessary for symbiotic response in root hairs (preprint article; Liang et al, 2020 ).…”

Section: Formation and Organization Of Nanodomainsmentioning

confidence: 99%

Membrane nanodomains and transport functions in plant

Martinière

Zelazny

2021

Plant Physiology

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Far from a homogenous environment, biological membranes are highly structured with lipids and proteins segregating in domains of different sizes and dwell times. In addition, membrane are highly dynamics especially in response to environmental stimuli. Understanding the impact of the nanoscale organization of membranes on cellular functions is an outstanding question. Plant channels and transporters are tightly regulated to ensure proper cell nutrition and signaling. Increasing evidence indicates that channel and transporter nano-organization within membranes plays an important role in these regulation mechanisms. Here, we review recent advances in the field of ion, water, but also hormone transport in plants, focusing on protein organization within plasma membrane nanodomains and its cellular and physiological impacts.

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Section: Formation and Organization Of Nanodomainsmentioning

confidence: 99%

Membrane nanodomains and transport functions in plant

Martinière

Zelazny

2021

Plant Physiology

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“…During cell signal transduction under physiological and pathological conditions, IDR creates diverse states of macromolecular assembly in spatiotemporally regulated manners, which could provide tunable activities of functional complexes, such as NF-NFPs. It has been well documented that phase separation dynamically regulates actin nucleator activities, such as the WASP and Arp2/3 complex during immune signaling (Su et al, 2016;Case et al, 2019) or plant formin during bacterial infection (Sun et al, 2018;Qiao et al, 2019;Ma and Miao, 2020;Ma et al, 2021a;Ma et al, 2021b;Sun et al, 2021). In both of the above scenarios, spatiotemporally regulated compositional stoichiometry plays a critical role in fine-tuning actin remodeling.…”

Section: Hierarchical Assembly Of Nucleation Complexes For Tunable Activitiesmentioning

confidence: 99%

A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae

Xie

Zhou

et al. 2022

MBoC

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Actin nucleation is achieved by collaborative teamwork of actin nucleator factors (NFs) and nucleation-promoting factors (NPFs) into functional protein complexes. Selective inter- and intramolecular interactions between the nucleation complex constituents enable diverse modes of complex assembly in initiating actin polymerization upon demand. Budding yeast has two formins, Bni1 and Bnr1, which are teamed up with different NPFs. However, the selective pairing between formin NFs and NPFs into the nucleation core for actin polymerization is not completely understood. By examining the functions and interactions of NPFs and NFs via biochemistry, genetics, and mathematical modeling approaches, we found that two NPFs, Aip5 and Bud6, showed joint teamwork effort with Bni1 and Bnr1, respectively, by interacting with the C-terminal intrinsically disordered region (IDR) of formin, in which two NPFs work together to promote formin-mediated actin nucleation. Although the C-terminal IDRs of Bni1 and Bnr1 are distinct in length, each formin IDR orchestrates the recruitment of Bud6 and Aip5 cooperatively by different positioning strategies to form a functional complex. Our study demonstrated the dynamic assembly of the actin nucleation complex by recruiting multiple partners in budding yeast, which may be a general feature for effective actin nucleation by formins. [Media: see text]

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“…Emerging evidence shows that inter-or intramolecular interactions of ABPs, including homo-and heterooligomeric interactions and lower-order to higher-order molecular assembly, are fundamental mechanisms in dynamic regulation of the biochemical activities of ABPs, such as during signal transduction, and thereby actin cytoskeleton polymerization and organization 63, . For example, during plant immune activation, intermolecular interactions between plant formin dimers on the plasma membrane enhance formin activities in actin nucleation, which plays a critical role in remodeling the actin cytoskeleton of plant cells upon bacterial infection 63,87,93 . In mammals, multivalent interactions between WASP and the Arp2/3 complex also activate actin nucleation during T-cell signal transduction [94][95][96] .…”

Section: Oligomerization Regulates the Biochemical Activities Of Abps In Actin Assemblymentioning

confidence: 99%

The Intrinsically Disordered Region of Coronins Fine-tunes Oligomerization and Actin Polymerization

Han

Surya

et al. 2022

Preprint

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Coronins are highly conserved actin-binding proteins (ABPs) in the eukaryotic kingdom for polymerizing actin cytoskeleton. The biochemical activity of coronins is primarily mediated by the structural N-terminal β-propeller and the C-terminal helical coiled-coil (CC) domains, but less is known about the function of a middle nonconserved region, the “unique region (UR)”. The coronin UR is an intrinsically disordered region (IDR). Herein, we demonstrate that the low complexity of the UR is a conserved signature of the coronin protein family, and the UR/IDR exhibits a striking evolutionary correlated pattern associated with sequence length. By analyzing the role of the IDR in coronins via coarse-grained simulations, we reveal that evolutionary selection of IDR length is coupled with the oligomerization of IDR-containing proteins (IDPs) to provide optimal functional output. By integrating biochemical and cell biology experiments and protein engineering, we found that the IDR regulates Crn1 biochemical activity, both in vivo and in vitro, by fine-tuning CC domain oligomerization and maintaining Crn1 in a tetrameric state. The IDR-guided optimization of Crn1 oligomerization is critical for Arp2/3-mediated actin polymerization.

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Formin nanoclustering-mediated actin assembly during plant flagellin and DSF signaling

Cited by 36 publications

References 107 publications

Membrane nanodomains and transport functions in plant

Membrane nanodomains and transport functions in plant

A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae

The Intrinsically Disordered Region of Coronins Fine-tunes Oligomerization and Actin Polymerization

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