Cell-to-Cell Connection in Plant Grafting – Molecular Insights into Symplasmic Reconstruction

2021 ◽  
Author(s):  
Ken-ichi Kurotani ◽  
Michitaka Notaguchi
Keyword(s):  
Cell Adhesion ◽  
Time Course ◽  
De Novo ◽  
Molecular Transport ◽  
Wound Response ◽  
Future Research ◽  
Sequencing Data ◽  
Graft Interface ◽  
Vascular Formation ◽  
Cell Cell

Abstract Grafting is a means to connect tissues from two individual plants and grow a single chimeric plant through establishment of both apoplasmic and symplasmic connections. Recent molecular studies using RNA-sequencing data have provided genetic information on the processes involved in tissue reunion, including wound response, cell division, cell-cell adhesion, cell differentiation, and vascular formation. Thus, studies on grafting increase our understanding of various aspects of plant biology. Grafting has also been used to study systemic signaling and transport of micro- and macromolecules in the plant body. Given that graft viability and molecular transport across graft junctions largely depend on vascular formation, a major focus in grafting biology has been the mechanism of vascular development. In addition, it has been thought that symplasmic connections via plasmodesmata are fundamentally important to share cellular information among newly proliferated cells at the graft interface and to accomplish tissue differentiation correctly. Therefore, this review focuses on plasmodesmata formation during grafting. We take advantage of interfamily grafts for unambiguous identification of the graft interface and summarize morphological aspects of de novo formation of plasmodesmata. Important molecular events are addressed by re-examining the time-course transcriptome of interfamily grafts, from which we recently identified the cell-cell adhesion mechanism. Plasmodesmata-associated genes upregulated during graft healing that may provide a link to symplasm establishment are described. We also discuss future research directions.

scholarly journals Cell–cell adhesion in plant grafting is facilitated by β-1,4-glucanases

2020 ◽  
Author(s):  
Michitaka Notaguchi ◽  
Ken-ichi Kurotani ◽  
Yoshikatsu Sato ◽  
Ryo Tabata ◽  
Yaichi Kawakatsu ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Fruit Trees ◽  
Living Tissue ◽  
Closely Related Species ◽  
Tomato Fruits ◽  
Diverse Range ◽  
Extracellular Region ◽  
Plant Families ◽  
Graft Interface ◽  
Cell Cell

Plant grafting is conducted for vegetative propagation in plants, whereby a piece of living tissue is attached to another tissue through establishment of cell–cell adhesion. Plant grafting has a long history in agriculture and has been applied to improve crop traits for thousands of years1. Plant grafting has mostly relied on the natural ability of a plant for wound healing. However, the compatibility of cell–cell adhesion typically limits graft combinations to closely related species2–4, and the mechanism by which cell–cell adhesion of injured tissues is established is largely unknown. Here, we show that a subclade of β-1,4-glucanases secreted into the extracellular region facilitates cell–cell adhesion near the graft interface. Nicotiana shows a propensity for cell–cell adhesion with a diverse range of angiosperms, including vegetables, fruit trees, and monocots, in which cell wall reconstruction was promoted in a similar manner to conventional intrafamily grafting5–7. Using transcriptomic approaches, we identified a specific clade of β-1,4-glucanases that is upregulated during grafting in successful graft combinations but not in incompatible grafts and precedes graft adhesion in inter- and intrafamily grafts. Grafting was facilitated with an overexpressor of the β-1,4-glucanase and, using Nicotiana stem as an interscion, we produced tomato fruits on rootstocks from other plant families. Our results demonstrate that the mechanism of cell–cell adhesion is partly conserved in plants and is a potential target to enhance plant grafting techniques.

scholarly journals Lipid Phosphate Phosphatase 3 Stabilization of β-Catenin Induces Endothelial Cell Migration and Formation of Branching Point Structures

2010 ◽  
Vol 30 (7) ◽  
pp. 1593-1606 ◽  
Author(s):  
Joseph O. Humtsoe ◽  
Mingyao Liu ◽  
Asrar B. Malik ◽  
Kishore K. Wary
Keyword(s):  
Cell Adhesion ◽  
Endothelial Cell ◽  
De Novo ◽  
Endothelial Cell Migration ◽  
Dependent Manner ◽  
P120 Catenin ◽  
Branching Point ◽  
Lipid Phosphate ◽  
Underlying Mechanisms ◽  
Cell Cell

ABSTRACT Endothelial cell (EC) migration, cell-cell adhesion, and the formation of branching point structures are considered hallmarks of angiogenesis; however, the underlying mechanisms of these processes are not well understood. Lipid phosphate phosphatase 3 (LPP3) is a recently described p120-catenin-associated integrin ligand localized in adherens junctions (AJs) of ECs. Here, we tested the hypothesis that LPP3 stimulates β-catenin/lymphoid enhancer binding factor 1 (β-catenin/LEF-1) to induce EC migration and formation of branching point structures. In subconfluent ECs, LPP3 induced expression of fibronectin via β-catenin/LEF-1 signaling in a phosphatase and tensin homologue (PTEN)-dependent manner. In confluent ECs, depletion of p120-catenin restored LPP3-mediated β-catenin/LEF-1 signaling. Depletion of LPP3 resulted in destabilization of β-catenin, which in turn reduced fibronectin synthesis and deposition, which resulted in inhibition of EC migration. Accordingly, reexpression of β-catenin but not p120-catenin in LPP3-depleted ECs restored de novo synthesis of fibronectin, which mediated EC migration and formation of branching point structures. In confluent ECs, however, a fraction of p120-catenin associated and colocalized with LPP3 at the plasma membrane, via the C-terminal cytoplasmic domain, thereby limiting the ability of LPP3 to stimulate β-catenin/LEF-1 signaling. Thus, our study identified a key role for LPP3 in orchestrating PTEN-mediated β-catenin/LEF-1 signaling in EC migration, cell-cell adhesion, and formation of branching point structures.

scholarly journals Rapid Suppression of Activated Rac1 by Cadherins and Nectins during De Novo Cell-Cell Adhesion

PLoS ONE ◽  
2011 ◽  
Vol 6 (3) ◽  
pp. e17841 ◽  
Author(s):  
Khameeka N. Kitt ◽  
W. James Nelson
Keyword(s):  
Cell Adhesion ◽  
De Novo ◽  
Cell Cell

scholarly journals Regulation of cell–cell adhesion by the cadherin–catenin complex

2008 ◽  
Vol 36 (2) ◽  
pp. 149-155 ◽  
Author(s):  
W. James Nelson
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Rho Gtpases ◽  
De Novo ◽  
Cytoplasmic Proteins ◽  
Cytoskeleton Reorganization ◽  
Dependent Cell ◽  
And Function ◽  
Cell Cell

Ca2+-dependent cell–cell adhesion is regulated by the cadherin family of cell adhesion proteins. Cadherins form trans-interactions on opposing cell surfaces which result in weak cell–cell adhesion. Stronger cell–cell adhesion occurs by clustering of cadherins and through changes in the organization of the actin cytoskeleton. Although cadherins were thought to bind directly to the actin cytoskeleton through cytoplasmic proteins, termed α- and β-catenin, recent studies with purified proteins indicate that the interaction is not direct, and instead an allosteric switch in α-catenin may mediate actin cytoskeleton reorganization. Organization and function of the cadherin–catenin complex are additionally regulated by phosphorylation and endocytosis. Direct studies of cell–cell adhesion has revealed that the cadherin–catenin complex and the underlying actin cytoskeleton undergo a series of reorganizations that are controlled by the Rho GTPases, Rac1 and RhoA, that result in the expansion and completion of cell–cell adhesion. In the present article, in vitro protein assembly studies and live-cell studies of de novo cell–cell adhesion are discussed in the context of how the cadherin–catenin complex and the actin cytoskeleton regulate cell–cell adhesion.

scholarly journals Multiple Cadherin Superfamily Members with Unique Expression Profiles Are Produced in Rat Testis1

Endocrinology ◽  
2000 ◽  
Vol 141 (2) ◽  
pp. 675-683 ◽  
Author(s):  
Kamin J. Johnson ◽  
Sutchin R. Patel ◽  
Kim Boekelheide
Keyword(s):  
Cell Adhesion ◽  
Messenger Rna ◽  
Time Course ◽  
Expression Profiles ◽  
Expression Patterns ◽  
Developmental Time ◽  
Pcr Cloning ◽  
Critical Function ◽  
Cadherin Superfamily ◽  
Cell Cell

Abstract Adhesion between germ and Sertoli cells is thought to be crucial for spermatogenesis. Cadherin superfamily proteins, including classic cadherins and protocadherins, are important mediators of cell-cell adhesion. Using a degenerate PCR cloning strategy, we surveyed the expression of cadherin superfamily members in rat testis. Similar to brain, testis expressed a large number of cadherin superfamily members: 7 classic cadherins of both types I and II, 14 protocadherins, 2 protocadherin-related cadherins, and 1 cadherin-related receptor-like protein. All three protocadherin families (α, β, and γ) were found in testis. Using a semiquantitative RT-PCR assay, messenger RNA expression was determined for each cadherin superfamily member during a postnatal developmental time-course and following ablation of specific testis cell types by ethanedimethanesulfonate, methoxyacetic acid, and 2,5-hexanedione. Diverse expression patterns were observed among the cadherins, suggesting that cadherin expression is cell type-specific in testis. The large number and variety of cadherin superfamily members found in testis supports a critical function for cadherin-mediated cell-cell adhesion in spermatogenesis.

scholarly journals Junctional actin assembly is mediated by Formin-like 2 downstream of Rac1

2015 ◽  
Vol 209 (3) ◽  
pp. 367-376 ◽  
Author(s):  
Katharina Grikscheit ◽  
Tanja Frank ◽  
Ying Wang ◽  
Robert Grosse
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Actin Polymerization ◽  
De Novo ◽  
Early Stage ◽  
Adhesion Formation ◽  
Actin Dynamics ◽  
Cell Contact ◽  
Actin Assembly ◽  
Cell Cell

Epithelial integrity is vitally important, and its deregulation causes early stage cancer. De novo formation of an adherens junction (AJ) between single epithelial cells requires coordinated, spatial actin dynamics, but the mechanisms steering nascent actin polymerization for cell–cell adhesion initiation are not well understood. Here we investigated real-time actin assembly during daughter cell–cell adhesion formation in human breast epithelial cells in 3D environments. We identify formin-like 2 (FMNL2) as being specifically required for actin assembly and turnover at newly formed cell–cell contacts as well as for human epithelial lumen formation. FMNL2 associates with components of the AJ complex involving Rac1 activity and the FMNL2 C terminus. Optogenetic control of Rac1 in living cells rapidly drove FMNL2 to epithelial cell–cell contact zones. Furthermore, Rac1-induced actin assembly and subsequent AJ formation critically depends on FMNL2. These data uncover FMNL2 as a driver for human epithelial AJ formation downstream of Rac1.

scholarly journals Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell–cell adhesion

2007 ◽  
Vol 178 (3) ◽  
pp. 517-527 ◽  
Author(s):  
Soichiro Yamada ◽  
W. James Nelson
Keyword(s):  
Cell Adhesion ◽  
Actin Filaments ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
De Novo ◽  
Actin Dynamics ◽  
Lateral Expansion ◽  
Actomyosin Contractility ◽  
Spatiotemporal Coordination ◽  
Cell Cell

Spatiotemporal coordination of cell–cell adhesion involving lamellipodial interactions, cadherin engagement, and the lateral expansion of the contact is poorly understood. Using high-resolution live-cell imaging, biosensors, and small molecule inhibitors, we investigate how Rac1 and RhoA regulate actin dynamics during de novo contact formation between pairs of epithelial cells. Active Rac1, the Arp2/3 complex, and lamellipodia are initially localized to de novo contacts but rapidly diminish as E-cadherin accumulates; further rounds of activation and down-regulation of Rac1 and Arp2/3 occur at the contacting membrane periphery, and this cycle repeats as a restricted membrane zone that moves outward with the expanding contact. The cortical bundle of actin filaments dissolves beneath the expanding contacts, leaving actin bundles at the contact edges. RhoA and actomyosin contractility are activated at the contact edges and are required to drive expansion and completion of cell–cell adhesion. We show that zones of Rac1 and lamellipodia activity and of RhoA and actomyosin contractility are restricted to the periphery of contacting membranes and together drive initiation, expansion, and completion of cell–cell adhesion.

scholarly journals Cell-cell adhesion in plant grafting is facilitated by β-1,4-glucanases

Science ◽  
2020 ◽  
Vol 369 (6504) ◽  
pp. 698-702 ◽  
Author(s):  
Michitaka Notaguchi ◽  
Ken-ichi Kurotani ◽  
Yoshikatsu Sato ◽  
Ryo Tabata ◽  
Yaichi Kawakatsu ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Living Tissue ◽  
Closely Related Species ◽  
Tomato Fruits ◽  
Diverse Range ◽  
Extracellular Region ◽  
Graft Compatibility ◽  
Plant Families ◽  
Graft Interface ◽  
Cell Cell

Plant grafting is conducted for fruit and vegetable propagation, whereby a piece of living tissue is attached to another through cell-cell adhesion. However, graft compatibility limits combinations to closely related species, and the mechanism is poorly understood. We found that Nicotiana is capable of graft adhesion with a diverse range of angiosperms. Comparative transcriptomic analyses on graft combinations indicated that a subclade of β-1,4-glucanases secreted into the extracellular region facilitates cell wall reconstruction near the graft interface. Grafting was promoted by overexpression of the β-1,4-glucanase. Using Nicotiana stem as an interscion, we produced tomato fruits on rootstocks from other plant families. These findings demonstrate that the process of cell-cell adhesion is a potential target to enhance plant grafting techniques.

scholarly journals Flow cytometric analysis and modeling of cell-cell adhesive interactions: the neutrophil as a model.

1990 ◽  
Vol 111 (6) ◽  
pp. 2747-2756 ◽  
Author(s):  
S I Simon ◽  
J D Chambers ◽  
L A Sklar
Keyword(s):  
Cell Adhesion ◽  
Time Course ◽  
Cell Function ◽  
Contact Region ◽  
Flow Cytometric Analysis ◽  
Second Phase ◽  
Aggregate Formation ◽  
Aggregation Rate ◽  
Adhesive Interactions ◽  
Cell Cell

The immune function of granulocytes, monocytes, lymphocytes, and other specialized cells depends upon intercellular adhesion. In many cases the molecules mediating leukocyte cell adhesion belong to the Leu-CAM superfamily of adhesive molecules. To elucidate the events of homotypic aggregation in a quantitative fashion, we have examined the aggregation of neutrophils stimulated with formyl peptides, where aggregate formation is a transient reversible cell function. We have mathematically modeled the kinetics of aggregation using a linear model based on particle geometry and rates of aggregate formation and breakup. The time course was modeled as a three-phase process, each phase with distinct rate constants. Aggregate formation was measured on the flow cytometer; singlets and larger particles were distinguished using the intravital stain LDS-751. Aggregation proceeded rapidly after stimulation with formyl peptide (CHO-nle-leu-phe-nle-tyr-lys). The first phase lasted 30-60 s; this was modeled with the largest aggregation rate and smallest rate of disaggregation. Aggregate formation plateaued during the second phase which lasted up to 2.5 min. This phase was modeled with an aggregation rate nearly an order of magnitude less than that of the initial fast phase, whereas the disaggregation rate for this phase did not change significantly. A third phase where disaggregation predominated, lasted the remaining 2-3 min and was modeled with a four to fivefold increase of the disaggregation rate. The mechanism of cell-cell adhesion in the plateau phase was probed with the monoclonal antibody IB4 to the CD18 subunit of the adhesive receptor CR3. Based on these studies it appears that new aggregates do not form to a large degree after the first phase of aggregate formation is complete. However, new adhesive contact sites may form within the contact region of these adherent cells to keep the aggregates together.

scholarly journals CADHERIN mediated AMIS localisation

2021 ◽  
Author(s):  
Xuan Liang ◽  
Antonia Weberling ◽  
Chun Yuan Hii ◽  
Magdalena Zernicka-Goetz ◽  
Clare E Buckley
Keyword(s):  
Cell Adhesion ◽  
Cell Division ◽  
De Novo ◽  
Embryonic Stem ◽  
Cellular Tissue ◽  
Initiation Site ◽  
Stage Of Development ◽  
Independent Mechanism ◽  
Epithelial Structure ◽  
Cell Cell

Individual cells within de novo polarising tubes and cavities must integrate their forming apical domains into a centralised apical membrane initiation site (AMIS). This is necessary to enable organised lumen formation within multi-cellular tissue. Despite the well documented importance of cell division in localising the AMIS, we have found a division-independent mechanism of AMIS localisation that relies instead on CADHERIN-mediated cell-cell adhesion. Our study of de novo polarising mouse embryonic stem cells (mESCs) cultured in 3D suggest that cell-cell adhesion directs the localisation of apical proteins such as PAR-6 to a centralised AMIS. Unexpectedly, we also found that mESC cell clusters lacking functional E-CADHERIN were still able to form a lumen-like cavity in the absence of AMIS localisation and did so at a later stage of development via a closure mechanism, instead of via hollowing. This work suggests that there are two, interrelated mechanisms of apical polarity localisation: cell adhesion and cell division. Alignment of these mechanisms in space allows for redundancy in the system and ensures the development of a coherent epithelial structure within a growing organ.

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