The <i>Drosophila</i> afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction

Sawyer, Jessica K.; Harris, Nathan; Slep, Kevin C.; Gaul, Ulrike; Peifer, Mark

doi:10.1083/jcb.200904001

Cited by 243 publications

(486 citation statements)

References 74 publications

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“…This suggests that other protein(s) stabilize Cno at this location (see below). (Sawyer et al, 2009). Interestingly, we found that Shg was present at the MG and was highly enriched, as is Cno, at the interface between the MG and commissural axons (Fig.…”

Section: Cno Forms a Complex In Vivo With Wrapper And Nrx-ivmentioning

confidence: 69%

Canoe functions at the CNS midline glia in a complex with Shotgun and Wrapper-Nrx-IV during neuron-glia interactions

Slováková

Carmena

2011

Development

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SUMMARYVertebrates and insects alike use glial cells as intermediate targets to guide growing axons. Similar to vertebrate oligodendrocytes, Drosophila midline glia ensheath and separate axonal commissures. Neuron-glia interactions are crucial during these events, although the proteins involved remain largely unknown. Here, we show that Canoe (Cno), the Drosophila ortholog of AF-6, and the DE-cadherin Shotgun (Shg) are highly restricted to the interface between midline glia and commissural axons. cno mutant analysis, genetic interactions and co-immunoprecipitation assays unveil Cno function as a novel regulator of neuronglia interactions, forming a complex with Shg, Wrapper and Neurexin IV, the homolog of vertebrate Caspr/paranodin. Our results also support additional functions of Cno, independent of adherens junctions, as a regulator of adhesion and signaling events in non-epithelial tissues.

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Section: Cno Forms a Complex In Vivo With Wrapper And Nrx-ivmentioning

confidence: 69%

Canoe functions at the CNS midline glia in a complex with Shotgun and Wrapper-Nrx-IV during neuron-glia interactions

Slováková

Carmena

2011

Development

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“…Inhibitors of nectin adhesion or afadin knockdown slow the formation of cadherin adhesive clusters in a Ca 2+ -switch assay (Sato et al, 2006;Lorger and Moelling, 2006) or between two cells upon coming into contact with one another (Indra et al, 2014). However, this defect in the kinetics of adherens junction formation does not affect the general appearance of cell-cell adhesion contacts, including the ultrastructural features of adherens junctions (Zhadanov et al, 1999;Sawyer et al, 2009;Tanaka-Okamoto et al, 2011). Therefore, the available data show that nectin facilitates the formation of adherens junctions, but it is involved neither in the basic mechanisms of their assembly nor in their structural organization.…”

Section: Introductionmentioning

confidence: 99%

Cadherin controls nectin recruitment into adherens junctions by remodeling the actin cytoskeleton

Troyanovsky

Indra

Chen

et al. 2014

Journal of Cell Science

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BSTRACTThe mechanism that coordinates activities of different adhesion receptors is poorly understood. We investigated this mechanism by focusing on the nectin-2 and E-cadherin adherens junction receptors. We found that, cadherin was not required for the basic process of nectin junction formation because nectin-2 formed junctions in cadherin-deficient A431D cells. Formation of nectin-2 junctions in these cells, however, became regulated by cadherin as soon as E-cadherin was re-expressed. E-cadherin recruited nectin-2 into adherens junctions, where both proteins formed distinct but tightly associated clusters. Live-cell imaging showed that the appearance of E-cadherin clusters often preceded that of nectin-2 clusters at sites of junction assembly. Inactivation of E-cadherin clustering by different strategies concomitantly suppressed the formation of nectin clusters. Furthermore, cadherin significantly increased the stability of nectin clusters, thereby making them resistant to the BC-12 antibody, which targets the nectin-2 adhesion interface. By testing different E-cadherin-a-catenin chimeras, we showed that the recruitment of nectin into chimera junctions is mediated by the actin-binding domain of a-catenin. Our data suggests that E-cadherin regulates assembly of nectin junctions through a-catenin-induced remodeling of the actin cytoskeleton around the cadherin clusters.

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“…This includes disorganization of the ectoderm, impaired migration of the mesoderm and loss of somites (Ikeda et al, 1999;Zhadanov et al, 1999). In Drosophila, afadin homolog Canoe (Cno) (Miyamoto et al, 1995) is essential during morphogenesis to maintain adherens junctions by connecting adherens junctions to actin (Sawyer et al, 2009). However, in contrast to mammals, Cno is dispensable for cadherin-catenin-based adherens junctions assembly and establishment of cell polarity in the fly (Sawyer et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

“…In Drosophila, afadin homolog Canoe (Cno) (Miyamoto et al, 1995) is essential during morphogenesis to maintain adherens junctions by connecting adherens junctions to actin (Sawyer et al, 2009). However, in contrast to mammals, Cno is dispensable for cadherin-catenin-based adherens junctions assembly and establishment of cell polarity in the fly (Sawyer et al, 2009). Cno contributes to regulate signal transduction during morphogenesis and genetically interacts with RAS, JNK, NOTCH and WNT pathways (Miyamoto et al, 1995;Takahashi et al, 1998;Matsuo et al, 1999;Boettner et al, 2003;Carmena et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Loss of AF6/afadin, a marker of poor outcome in breast cancer, induces cell migration, invasiveness and tumor growth

et al. 2011

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Afadin/AF6, an F-actin-binding protein, is ubiquitously expressed in epithelia and has a key role during development, through its regulatory role in cell-cell junction organization. Afadin loss of expression in 15% of breast carcinoma is associated with adverse prognosis and increased risk of metastatic relapse. To determine the role of afadin in breast cancer, we studied the functional consequences of afadin protein extinction using in vitro and in vivo models. Three different breast cancer cell lines representative of the major molecular subtypes were stably repressed for afadin expression (knockdown of afadin (afadin KD)) using RNA interference. Collective and individual migrations as well as Matrigel invasion were markedly increased in afadin KD cells. Heregulin-b1 (HRG-b1)-induced migration and invasion were increased by twofold in afadin KD cells. Conversely, ectopic expression of afadin in the afadin-negative T47D cell line inhibited spontaneous and HRG-b1-induced migrations. RAS/MAPK and SRC kinase pathways were activated in afadin KD cells. Activation levels positively correlated with migration and invasion strength. Use of MEK1/2 (U0126) and SRC kinases (SU6656) inhibitors reduced afadin-dependent migration and invasion. Afadin extinction in the SK-BR-3 cell line markedly accelerated tumor growth development in mouse mammary gland and lung metastasis formation. These results may explain why the loss of afadin expression in tumors correlates with high tumor size and poor metastasis-free survival in patients.

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The Drosophila afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction

Cited by 243 publications

References 74 publications

Canoe functions at the CNS midline glia in a complex with Shotgun and Wrapper-Nrx-IV during neuron-glia interactions

Canoe functions at the CNS midline glia in a complex with Shotgun and Wrapper-Nrx-IV during neuron-glia interactions

Cadherin controls nectin recruitment into adherens junctions by remodeling the actin cytoskeleton

Loss of AF6/afadin, a marker of poor outcome in breast cancer, induces cell migration, invasiveness and tumor growth

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