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Wang, J.;  Lian, N.;  Zhang, Y.;  Man, Y.;  Chen, L.;  Yang, H.;  Lin, J.;  Jing, Y. Cytoskeletal Remodeling during Plant Immunity. Encyclopedia. Available online: https://encyclopedia.pub/entry/39154 (accessed on 19 July 2025).
Wang J,  Lian N,  Zhang Y,  Man Y,  Chen L,  Yang H, et al. Cytoskeletal Remodeling during Plant Immunity. Encyclopedia. Available at: https://encyclopedia.pub/entry/39154. Accessed July 19, 2025.
Wang, Jingyi, Na Lian, Yue Zhang, Yi Man, Lulu Chen, Haobo Yang, Jinxing Lin, Yanping Jing. "Cytoskeletal Remodeling during Plant Immunity" Encyclopedia, https://encyclopedia.pub/entry/39154 (accessed July 19, 2025).
Wang, J.,  Lian, N.,  Zhang, Y.,  Man, Y.,  Chen, L.,  Yang, H.,  Lin, J., & Jing, Y. (2022, December 23). Cytoskeletal Remodeling during Plant Immunity. In Encyclopedia. https://encyclopedia.pub/entry/39154
Wang, Jingyi, et al. "Cytoskeletal Remodeling during Plant Immunity." Encyclopedia. Web. 23 December, 2022.
Cytoskeletal Remodeling during Plant Immunity
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This entry is adapted from the peer-reviewed paper 10.3390/ijms232415553

The plant cytoskeleton, consisting of actin filaments and microtubules, is a highly dynamic filamentous framework involved in plant growth, development, and stress responses. Recently, research has demonstrated that the plant cytoskeleton undergoes rapid remodeling upon sensing pathogen attacks, serving as an important platform for responding to pathogen infections. Meanwhile, pathogens produce effectors targeting the cytoskeleton to achieve pathogenicity. 

actin filament microtubule plant immunity dynamics

1. Introduction

A large number of pathogenic microorganisms exist in the environment in which plants live. In order to counter the invasion by pathogens, plants have evolved two tiers of defense systems. Pattern-triggered immunity (PTI) is the first layer, generally activated by the perception of pathogen- or microbe-associated molecular patterns (PAMPs/MAMPs) and self-released damage-associated molecular patterns (DAMPs) via pattern-recognizing receptors (PRRs) [1][2][3]. This is often accompanied by an increased intracellular calcium concentration, bursts of reactive oxygen species (ROS), accretion of the lipid molecule, activation of mitogen-activated protein kinases (MAPKs), etc. These messengers trigger downstream reactions and fine-tune cellular signaling networks in plant immunity [3][4]. However, many pathogens have adapted to this mechanism and evolved effectors to bypass or straightly repress PTI [5]. Plants have also developed intracellular resistance proteins, i.e., nucleotide-binding leucine-rich repeat receptors (NLRs), that recognize bacterial effectors and usually cause a hypersensitive response (HR) to impede the pathogen spread, thus leading to effector-triggered immunity (ETI), which is the second layer of plant immunity [2][6].
The plant cytoskeleton, composed of microtubules and actin filaments, is a highly dynamic structure in cells and participates in many physiological activities, for instance, material transport, organelle movement, and cell division. In addition, the cytoskeleton also acts as a regulator of plant tolerance to biotic and abiotic stresses [7][8][9]. Microtubules are hollow tubular structures assembled from tubulin proteins, each composed of two globulin subunits that form a heterodimer. Meanwhile, actin filaments are composed of actin, usually forming a twisted chain about 7 nm in diameter. Microtubules and actin filaments are highly dynamic and undergo active polymerization and depolymerization processes, which are usually regulated by cytoskeleton-associated proteins, including microtubule-associated proteins (MAPs) and actin-binding proteins (ABPs), through nucleation of new filaments and polymerization, bundling, severing, and depolymerization of cytoskeletal fibers [7][10].
Recently, the cytoskeleton has been found to reorganize after pathogen attacks. This remodeling of the cytoskeleton is considered to serve as a platform for the perception and transduction of signals in the plant immune response, among which the function of actin filaments in plant immunity has been well-studied [9][11][12]. Meanwhile, the cytoskeleton also acts as the target of effectors produced by pathogens, making the interaction between host plants and pathogens more complex. Many ABPs have been identified to be necessary for actin cytoskeletal remodeling during the immune response [9][13][14][15]. Moreover, there are also some reports on the involvement of microtubules during the plant defense response [11].

2. The Cytoskeleton Undergoes Remodeling during PTI

The increase in the density of actin filaments in epidermal pavement cells is a conserved feature of the PTI response [16]. The actin filament density increases in plants in response to fungal, oomycete, and bacterial infection, but the rearrangement of actin filaments varies with different types of pathogens. When plants respond to fungal and oomycete infections, actin filaments increase at the site where pathogens try to enter [17][18][19]. Pathogenic fungi can develop a unique structure named the appressorium during the invasion of plants, which can penetrate the periclinal wall of the host cells [20][21]. In a recent study, it was found that the actin filaments of Arabidopsis leaf epidermal cells change accordingly after being infected by the barley powdery mildew fungus Blumeria graminis f. sp. hordei (Bgh) [13]. In the early stage of infection, cortical actin filaments in leaf epidermal cells frequently accumulate around the invasion site with an increased density, forming concentrated, dome-like patches surrounding the penetration site. These actin patches appear to be less susceptible to treatment with the actin-depolymerizing drug latrunculin A (LatA), indicating that the filaments of actin patches at the penetration sites possess a higher stability [13]. In the late stage, polarized cytoplasmic actin filament bundles pass through the infected cell toward the site of penetration, displaying highly dynamic properties, and are gradually disintegrated at a later time [13]. The rearrangement of the actin cytoskeleton in epidermal cells during the infection of oomycetes is somewhat similar to that during the infection of fungi. Likewise, in the interaction of Arabidopsis with Phytophthora sojae and Peronospora parasitica, actin filaments reorganize to form large bundles at the site of oomycete infection [19]. This actin rearrangement after the perception of fungi and oomycetes facilitates the transport of defense compounds or proteins to pathogen attack sites, preventing pathogen invasion [13][14][22]. Genetic or chemical disruption of the actin cytoskeleton makes plants more sensitive to fungal pathogens and affects the accumulation of defense signaling molecules at the infection sites [23][24][25][26]. Unlike fungi and oomycetes, bacteria usually colonize on leaf surfaces or enter into the host mesophyll tissues through wounds or stomata and proliferate in this region [27][28]. Thus, the increase in actin filament density does not just exist locally. In Arabidopsis cotyledons inoculated with Pseudomonas syringae pv. tomato DC3000 (Pst DC3000) or the T3SS-deficient mutant hrpH, an elevated actin filament abundance was observed in the cortical cytoplasm of epidermal cells 6 h after inoculation. This early increase in actin filaments density is relevant to PTI [16]. In the case of bacterial pathogen perception, Henty-Ridilla et al. reported that disruption of the actin cytoskeleton with Latrunculin B (LatB) increased the Arabidopsis susceptibility to Pst DC3000 infection. However, there are also reports that LatB pretreatment enhanced Arabidopsis resistance to Pst DC3000 as well as Brassica napus resistance to Leptosphaeria maculans, reflecting the complexity of interactions between pathogenic bacteria and plant cytoskeleton [16][29]. Moreover, treatment of Arabidopsis leaves with both the flagellin peptide flg22 and the fungal cell wall component chitin can induce an increase in actin filament density as well. This process requires recognition of the signal by the corresponding receptor and downstream signal components, indicating that MAMP treatment is sufficient to cause changes in the actin arrangement in epidermal cells [16]. It was found that the treatment of hypocotyls with MAMPs induced alterations in the dynamics of individual actin filaments in epidermal cells [30][31]. In mock-treated cells, actin filaments can be divided into three types of origin: generated from the cytoplasm, generated at the ends of preexisting filaments, or generated at the sides of preexisting filaments. These three nucleation events are roughly equal in proportion. In conserved 26–amino acid peptide from bacterial elongation factor - (elf26) or chitin-treated cells, some kinetic parameters are changed. In elf26-treated cells, filaments tend to nucleate laterally, while in chitin-treated cells, they tend to nucleate terminally. In addition, the average length and lifetimes of actin filaments increase significantly, the frequency of filament–filament annealing increases, and severing decreases, but the elongation and regeneration rates do not change significantly [30][31]. As a result, the actin filament abundance in cells is increased. Hence, the increased density of actin filaments may be owing to changes in the dynamics of individual actin filaments.
In addition to epidermal pavement cells, stomata are also important gateways for pathogens to enter plants, which are often closed during plant immunity to prevent pathogens from entering. This process is called stomatal immunity, which is a part of plant innate immunity [32][33]. Stomatal movement is related to actin cytoskeleton dynamics. Actin filaments are arranged radially in open stomata, while in closed stomata, the actin cytoskeleton is mainly aligned longitudinally. Unlike in epidermal cells, Pst DC3000 infection does not change the abundance of actin filaments in Arabidopsis guard cells, but it affects the orientation of actin filaments. After sensing Pst DC3000, the actin filaments in stomata changes from a radial to a longitudinal arrangement, consistent with stomatal closure. However, the increase in actin filament density and bundling found in epidermal pavement cells is not observed during this process [34]. There are different reports on MAMP-induced actin rearrangement in guard cells. Shimono et al. found that both flg22 and chitin treatment induced stomatal closure, but the state of actin filaments was dominated by radial bundles. Meanwhile Zou et al. discovered that flg22 induced a decrease in the dynamicity of actin filaments, and the status of the actin filament distribution was randomly or longitudinally dominated. In both cases, no significant changes in actin filament density were detected [15][34]. The dynamics of the actin cytoskeleton in guard cells during the immune response as well as the involved regulation mechanisms still require further examination.
Microtubules also rearrange during pathogen infection, and disturbance of microtubules using chemical drugs or genetic methods increases plant sensitivity to pathogens, suggesting that changes in the microtubule cytoskeleton represent a portion of the plant defense response [9]. Interestingly, unlike the relatively consistent response of actin filaments in response to pathogens, the microtubule cytoskeleton appears to exhibit a variety of dynamic behaviors in different host–host interactions: some are aligned radially below the appressoria, some exhibit local microtubule depolymerization at the contact site of pathogens, and some show a circumferential arrangement [11]. For example, microtubules rarely aggregated or rearranged at the site of infection when Arabidopsis was attacked by Bgh, and no polar array of microtubules was observed in the later infection stage, suggesting that microtubules participate less in modulating focal cellular responses during the interaction between Arabidopsis and powdery mildew [13]. On the contrary, microtubules polarized at the infection site were observed in the interaction between barley and Bgh. In cells that the fungus succeeded in penetrating, microtubules loosened [35]. Hence, microtubules reorganize during the plant defense response, but the manner of rearrangement varies by plant and pathogen species. More studies are needed in the future to explore the detailed role of microtubules in plant immunity.
Besides the infection of pathogenic bacteria, nematode infections also affect the cytoskeletal organization of host plants. Root knot nematodes and cyst nematodes are the main nematodes that infect plants [11]. During infection, root knot nematodes form a multi-nucleated giant cell structure, usually consisting of six host cells, while cyst nematodes form syncytia [11][36]. In Arabidopsis syncytia, actin filaments and microtubules were found to be disrupted, and the mitotic apparatus was not observed. However, in giant cells, the mitotic apparatus was found, but the actin and cortical microtubules were disturbed. The depolymerization of the actin or microtubule cytoskeleton by chemical drugs causes nearly normal maturation of the infecting nematode, indicating that the disruption of the cytoskeleton is probably a necessity to allow nematodes to complete their life [37]. Thus, the cytoskeleton is also involved in the process of nematode infection.

3. Cytoskeletal Remodeling in ETI and Effectors Targeting the Cytoskeleton

The cytoskeleton also undergoes rearrangement during the ETI response. Pst DC3000 and not the T3SS-deficient mutant hrpH induces significant actin bundles 24 h after inoculation [16]. This illustrates that the formation of actin bundles in the late stage of bacterial infection is correlated with ETI. Researchers have found that many pathogens have evolved effectors that act on the cytoskeleton to enhance colonization (Figure 1A). Bacterial effectors that have been found to affect the cytoskeleton are listed in Table 1.
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Figure 1. Regulation of actin filament dynamics in epidermal cells during plant immunity. (A) Sensing of bacteria induces actin filament remodeling, while bacteria produce effectors targeting the cytoskeleton. (B) When pathogens infect plants, PM-located PRRs are activated after sensing the corresponding PAMPs/MAMPs/DAMPs. PRRs activation induces the aggregation of type-I formin in membrane microdomains and promotes actin filament nucleation and assembly. (C) PRF3, which negatively regulates actin polymerization, is degraded after PRRs are activated. (D) During fungal infection, the ARP2/3 complex and type-I formin cooperate to form actin patches. (E,F) Upon sensing pathogens, PA levels are elevated through the activation of PLDβ, which further induces ROS production and inhibits CP activity. PLDβ binds F-actin and positively regulates its activity. (G) The activation of PRRs is often accompanied by an increased intracellular calcium concentration. (H) Calcium-dependent protein kinase 3 (CPK3) decodes calcium signal and phosphorylates ADF4 to separate it from actin filaments. (I) Changes in the actin filament density negatively regulate ROS production, probably through the modulation of PLDβ activity. (J) In addition, effectors released by bacteria break the actin cytoskeleton, which may improve plant resistance by increasing SA production. (K) Phosphorylated ADF4 is necessary for RPS5 expression, but the mechanism is still unclear. Solid lines indicate known or direct interactions, while dashed lines indicate unknown or indirect interactions. Arrows indicate the activation of signaling, while bars indicate an inhibitory effect. PRRs, pattern-recognizing receptors; PAMPs, pathogen-associated molecular patterns; MAMPs, microbe-associated molecular patterns; DAMPs, damage-associated molecular patterns. CW, cell wall; PM, plasma membrane.
HopW1 is a bacterial effector from Pst DC3000 that targets the actin cytoskeleton. It interacts with AtACT7, reduces actin filamentous networks, and inhibits endocytosis. Expressing HopW1 in plants destroys the actin cytoskeleton, resulting in undetectable Lifeact-GFP-labeled actin filaments [38][39]. Another effector from Pst DC3000, HopG1, induces structural changes in actin filaments during infection. HopG1 was associated with actin bundling 24 h after infection. Loss of hopG1 in Pst DC3000 results in reduced actin bundling and increased actin filaments in Arabidopsis. HopG1 disrupts actin stability and is associated with etiolation induction during infection [40]. Further studies have shown that HopG1 interacts with the mitochondrial-localized kinesin and is indirectly linked to actin through this interaction. Moreover, Arabidopsis kinesin mutants have reduced sensitivity to Pst DC3000 [40]. Previously, a kinesin-like calmodulin-binding protein was revealed to contain the MyTH4-FERM domain, allowing it to bind to both actin filaments and microtubules, suggesting that kinesin may dually bind microtubules and actin filaments [41]. Based on these results, it is hypothesized that HopG1-targeted kinesin is the mechanism that induces actin bundling during pathogen infection, thus inducing chlorosis and the formation of disease symptoms [40]. XopR, containing many disordered residues and potential plasma-membrane- and actin-binding motifs, is a newly identified effector of Xanthomonas campestris. During the early stage of infection, XopR goes through liquid–liquid phase separation (LLPS) via intrinsically disordered region (IDR)-mediated interactions, which recruits and condenses formin dimers into surface nanoclusters, promoting actin nucleation. In the late stage of infection, high concentrations of XopR cause formin to form large aggregates, inhibiting nucleation, promoting the formation of F-actin bundles, and reducing depolymerization by competing with actin depolymerizing factor (ADF) to bind actin [42].
In addition to targeting the actin cytoskeleton, many effectors have been identified to act upon microtubules in plant cells. Some of them directly destroy microtubule networks, and some target MAPs [43]. HopZ1a has acetyltransferase activity that interacts with and acetylates microtubules, leading to disruption of microtubule networks during late infection, interfering with secretion, affecting callose deposition, and blocking cell-wall-based defenses to enhance virulence [44]. HopE1 targets AtMAP65-1, a microtubule-associated protein that bundles microtubules, and dissociates it from the microtubule, disrupting the secretion of immune-related proteins. Atmap65-1 mutants were more sensitive to Pst DC3000 and were deficient in the secretion of the immunity protein PR-1, suggesting that AtMAP65-1 plays a major part in plant immunity and protein secretion. However, the mechanism by which HopE1 dissociates MAP65-1 from microtubules and its effect on the microtubule network are still unclear and need to be further studied [45]. AvrBsT delivered into cells by Pst DC3000′s T3S system interacts with AtACIP1, which co-locates with microtubules in cells. AvrBsT infection induces the organization of large GFP-AtACIP1 aggregates dependent on an acetyltransferase activity, which is assumed to play a function in microtubule reorganization and microtubule-based processes [46]. The effector XopL is an E3 ubiquitin ligase, and its mutant lacking E3 ubiquitin ligase activity is selectively distributed to the microtubules. The filaments labeled by mutant XopL are usually aligned with stromules. Meanwhile, XopL inhibits stromule elongation and induces plastid aggregation. It is assumed that microtubules may be one of the targets of XopL. However, the precise effect of XopL on microtubules should be further investigated [47].
Table 1. Bacterial effectors targeting the cytoskeleton.
Pathogen Effector Activity Target Function References
Pseudomonas syringae HopW1 Unknown Actin Disruption of F-actin; inhibition of protein trafficking and endocytosis [38][39]
Pseudomonas syringae HopG1 Unknown Mitochondrial-
localized kinesin; indirectly associated with actin		 Induction of actin bundling; induction of chlorosis [40]
Xanthomonas campestris XopR Nucleation Formin; actin Activation of formin-mediated nucleation during early infection; promotes the formation of F-actin bundles and inhibits actin nucleation and depolymerization during late infection [42]
Pseudomonas syringae HopZ1a Acetyltransferase Tubulin Acetylation and depolymerization of microtubules; inhibition of secretory [44]
Pseudomonas syringae HopE1 Unknown AtMAP65-1 Dissociates AtMAP65-1 from microtubules; inhibits the secretion of immune-related proteins [45]
Xanthomonas euvesicatoria AvrBsT Acetyltransferase AtACIP1, which co-locates with microtubules Acetylation of AtACIP1; induces the formation of AtACIP1 aggregates, which probably affect microtubule assembly [46]
Xanthomonas campestris XopL E3 ubiquitin ligase Unknown, probably microtubules Inhibits stromule elongation; induces plastid aggregation [47]
Nematodes also secrete effectors that destroy the cytoskeleton. It was found that MiPFN3 (Meloidogyne incognita Profilin 3), an effector secreted by root knot nematodes, can bind to actin monomers, disrupt actin polymerization, and reduce the filamentous actin network [36]. Manipulation of the cytoskeleton by nematodes may be a strategy to promote parasitism.

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Subjects: Plant Sciences
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register :
Jingyi Wang
,
Na Lian
,
Yue Zhang
,
Yi Man
,
Lulu Chen
,
Haobo Yang
,
Jinxing Lin
,
Yanping Jing
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