Cytoskeleton Interactions Involved in the Assembly and Function of Glycoprotein-80 Adhesion Complexes in Dictyostelium

Harris, Tony; Ravandi, Amir; Awrey, Donald E.; Siu, Chi‐Hung

doi:10.1074/jbc.m206241200

Cited by 14 publications

(5 citation statements)

References 56 publications

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“…Gp80 and ponticulin form the basis of a cell-cell adhesion system (Hitt et al, 1994;Harris et al, 2003), whereas filopodin (talin), an integrin ␤-like protein, and sadA are involved in cell-substrate adhesion (Simson et al, 1998;Fey et al, 2002;Cornillon et al, 2006). Significantly, enlazin, cortexillin-I, and filopodin (talin) have quantitative effects on both adhesion and cortical mechanics (Simson et al, 1998;Girard et al, 2004; this study).…”

Section: Cell Adhesion In Dictyosteliummentioning

confidence: 63%

Enlazin, a Natural Fusion of Two Classes of Canonical Cytoskeletal Proteins, Contributes to Cytokinesis Dynamics

Octtaviani¹,

Effler²,

Robinson³

2006

MBoC

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Cytokinesis requires a complex network of equatorial and global proteins to regulate cell shape changes. Here, using interaction genetics, we report the first characterization of a novel protein, enlazin. Enlazin is a natural fusion of two canonical classes of actin-associated proteins, the ezrin-radixin-moesin family and fimbrin, and it is localized to actin-rich structures. A fragment of enlazin, enl-tr, was isolated as a genetic suppressor of the cytokinesis defect of cortexillin-I mutants. Expression of enl-tr disrupts expression of endogenous enlazin, indicating that enl-tr functions as a dominantnegative lesion. Enlazin is distributed globally during cytokinesis and is required for cortical tension and cell adhesion. Consistent with a role in cell mechanics, inhibition of enlazin in a cortexillin-I background restores cytokinesis furrowing dynamics and suppresses the growth-in-suspension defect. However, as expected for a role in cell adhesion, inhibiting enlazin in a myosin-II background induces a synthetic cytokinesis phenotype, frequently arresting furrow ingression at the dumbbell shape and/or causing recession of the furrow. Thus, enlazin has roles in cell mechanics and adhesion, and these roles seem to be differentially significant for cytokinesis, depending on the genetic background.

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Section: Cell Adhesion In Dictyosteliummentioning

confidence: 63%

Enlazin, a Natural Fusion of Two Classes of Canonical Cytoskeletal Proteins, Contributes to Cytokinesis Dynamics

Octtaviani¹,

Effler²,

Robinson³

2006

MBoC

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“…Cishomodimers and oligomers are formed if the molecules have affinity for each other. In the case of D. discoideum, the cell-adhesion protein csA/gp80 is anchored in the plasma membrane through a lipid moiety [41] and oligomers of csA/gp80 are sequestered in lipid rafts, which facilitate the rapid expansion of adhesion complexes [42][43][44]. In addition to direct protein-protein interactions, cells may utilize lipid rafts in the assembly of adhesion complexes [40].…”

Section: Discussionmentioning

confidence: 99%

Assembly of the TgrB1–TgrC1 cell adhesion complex during Dictyostelium discoideum development

Chen

et al. 2014

Biochemical Journal

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In Dictyostelium discoideum, TgrB1 and TgrC1 are partners of a heterophilic cell-adhesion system. To investigate its assembly process, the split GFP complementation assay was used to track the oligomeric status of both proteins. The ability of TgrC1 to form cis-homodimers spontaneously was demonstrated by fluorescence complementation studies and confirmed by chemical cross-linking. In contrast, TgrB1 failed to form cis-homodimers in the absence of TgrC1. Treatment of cell aggregates with antibodies against TgrB1 or TgrC1 did not affect TgrC1 dimerization, but inhibited TgrB1 dimer formation, suggesting that TgrB1 cis-homodimerization is dependent on trans-interaction with TgrC1. When TgrB1 and TgrC1 conjugated with the complementary halves of GFP were co-expressed in cells, cis-heterodimers were not detected. However, weak FRET signals were detected in cells expressing TgrB1-RFP and TgrC1-GFP, suggesting that TgrB1 dimers and TgrC1 dimers were arranged juxtapose to each other in the adhesion complex. The results of the present study suggest that the assembly process is initiated upon trans-interaction of monomeric TgrB1 with TgrC1 homodimers on adjacent cells, which triggers the formation of TgrB1 dimers. The homodimerization of TgrB1 in turn induces the clustering of TgrB1 and TgrC1, and the coalescence of TgrB1-TgrC1 clusters results in the formation of large adhesion complexes.

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“…4B), and they can be isolated as a Triton‐insoluble floating membrane fraction or low‐density membrane fragments after sonication of the plasma membrane. Interestingly, studies of this assembly process in ponticulin‐null cells suggest that it can occur without contribution from the actin cytoskeleton (Harris et al. 2003).…”

Section: Coordinated Appearance Of Ddcad‐1 and Csa/gp80 During Cell Amentioning

confidence: 99%

Regulation of spatiotemporal expression of cell–cell adhesion molecules during development of Dictyostelium discoideum

Siu¹,

Sriskanthadevan²,

Wang³

et al. 2011

Dev Growth Differ

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The social amoeba Dictyostelium discoideum is a simple but powerful model organism for the study of cell-cell adhesion molecules and their role in morphogenesis during development. Three adhesive systems have been characterized and studied in detail. The spatiotemporal expression of these adhesion proteins is stringently regulated, often coinciding with major shifts in the morphological complexity of development. At the onset of development, amoeboid cells express the Ca 2+-dependent cell-cell adhesion molecule DdCAD-1, which initiates weak homophilic interactions between cells and assists in the recruitment of individuals into cell streams. DdCAD-1 is unique because it is synthesized as a soluble protein in the cytoplasm. It is targeted for presentation on the cell surface by an unconventional protein transport mechanism via the contractile vacuole. Concomitant with the aggregation stage is the expression of the contact sites A glycoprotein csA ⁄ gp80 and TgrC1, both of which mediate Ca 2+ ⁄ Mg 2+-independent cell-cell adhesion. Whereas csA ⁄ gp80 is a homophilic binding protein, TgrC1 binds to a heterophilic receptor on the cell. During cell aggregation, csA ⁄ gp80 associates preferentially with lipid rafts, which facilitate the rapid assembly of adhesion complexes. TgrC1 is synthesized at low levels during aggregation and rapid accumulation occurs initially in the peripheral cells of loose mounds. The extracellular portion of TgrC1 is shed and becomes part of the extracellular matrix. Additionally, analyses of knockout mutants have revealed important biological roles played by these adhesion proteins, including size regulation, cell sorting and cell-type proportioning.

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Cytoskeleton Interactions Involved in the Assembly and Function of Glycoprotein-80 Adhesion Complexes in Dictyostelium

Cited by 14 publications

References 56 publications

Enlazin, a Natural Fusion of Two Classes of Canonical Cytoskeletal Proteins, Contributes to Cytokinesis Dynamics

Enlazin, a Natural Fusion of Two Classes of Canonical Cytoskeletal Proteins, Contributes to Cytokinesis Dynamics

Assembly of the TgrB1–TgrC1 cell adhesion complex during Dictyostelium discoideum development

Regulation of spatiotemporal expression of cell–cell adhesion molecules during development of Dictyostelium discoideum

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