The many faces of cell adhesion during Drosophila muscle development

Maartens, Aidan; Brown, Nicholas H.

doi:10.1016/j.ydbio.2014.12.038

Cited by 56 publications

(72 citation statements)

References 175 publications

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“…In the embryo, Kon and αPS2βPS integrin are both present on the muscle side of the MTJ (Estrada et al, 2007;Maartens and Brown, 2015). To gain insight into the mechanism underlying the interaction between Kon and integrin, we analyzed whether integrin function was affected in the absence of Kon.…”

Section: Kon Is Essential For αPs2βps Integrin Signaling At the Musclmentioning

confidence: 99%

“…Cells can adhere to each other directly or indirectly through the adhesion to the extracellular matrix (ECM) surrounding them (Rozario and DeSimone, 2010). This is mainly achieved by the transmembrane integrin receptors (Brown, 2000;Maartens and Brown, 2015) although it can also be mediated by other receptors such as Dystroglycan (Bozzi et al, 2009) and other proteoglycan receptors (Couchman, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…The construction of the MTJ involves the coordinated development and crosstalk between tendons and muscles (Maartens and Brown, 2015;Schweitzer et al, 2010). During MTJ formation, different cellular processes take place in a timely manner, such as cell specification, muscle migration toward tendons, and muscle-tendon recognition and attachment.…”

Section: Introductionmentioning

confidence: 99%

“…Different integrins interact with distinct types of ECM proteins: αPS1βPS interacts with laminin (Gotwals et al, 1994), whereas αPS2βPS interacts with Thrombospondin (Tsp) and Tiggrin (Bunch et al, 1998;Chanana et al, 2007;Fogerty et al, 1994;Subramanian et al, 2007). In fact, controlling the right levels of these ECM molecules is key to the formation of the MTJ (Gilsohn and Volk, 2010;Maartens and Brown, 2015;Yatsenko and Shcherbata, 2014). In particular, the role of Tsp in the MTJ has been studied in detail.…”

Section: Introductionmentioning

confidence: 99%

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Kon-tiki enhances PS2 integrin adhesion and localizes its ligand, Thrombospondin, in the myotendinous junction

Pérez-Moreno

Espina-Zambrano

García-Calderón

et al. 2017

Journal of Cell Science

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Cell-extracellular-matrix adhesion is mediated by cell receptors, mainly integrins and transmembrane proteoglycans, which can functionally interact. How these receptors are regulated and coordinated is largely unknown. We show that the conserved transmembrane Drosophila proteoglycan Kon-tiki (Kon, also known as Perdido) interacts with the αPS2βPS integrin (αPS2 is encoded by inflated and βPS by myospheroid) to mediate muscle-tendon adhesion. kon and inflated double mutant embryos show a synergistic increase in muscle detachment. Furthermore, Kon modulates αPS2βPS signaling at the muscle attachment, since phosphorylated Fak is reduced in kon mutants. This reduction in integrin signaling can be rescued by the expression of a truncated Kon protein containing its transmembrane and extracellular domains, suggesting that these domains are sufficient to mediate this signaling. We show that these domains are sufficient to properly localize the αPS2βPS ligand, Thrombospondin, to the muscle attachment, and to partially rescue Kon-dependent muscle-tendon adhesion. We propose that Kon can engage in a protein complex with αPS2βPS and enhance integrin-mediated signaling and adhesion by recruiting its ligand, which would increase integrin-binding affinity to the extracellular matrix, resulting in the consolidation of the myotendinous junction.

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Section: Kon Is Essential For αPs2βps Integrin Signaling At the Musclmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Kon-tiki enhances PS2 integrin adhesion and localizes its ligand, Thrombospondin, in the myotendinous junction

Pérez-Moreno

Espina-Zambrano

García-Calderón

et al. 2017

Journal of Cell Science

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“…Targeting of embryonic muscle toward tendon cells relies on the Slit-Robo system, the leucine-rich tendon specific protein (Lrt), and the matrix proteins Thrombospondin (Tsp) and Slowdown (CHANANA et al 2007;SUBRAMANIAN et al 2007;WAYBURN and VOLK 2009;VOLK 2010a, 2010b). Attachment initiates with the secretion of extracellular matrix components, including Tsp and laminin, and accumulation of integrins at myotube and tendon membranes (SUBRAMANIAN et al 2007;MAARTENS and BROWN 2015). Subsequently, a few hours later, myofibrillogenesis begins, driving myotube compaction, which in turn pulls tendon cells inside the thoracic cavity (METCALFE 1970;OLGUIN et al 2011;.…”

mentioning

confidence: 99%

Establishment of the Muscle–Tendon Junction During Thorax Morphogenesis in Drosophila Requires the Rho-Kinase

et al. 2016

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The assembly of the musculoskeletal system in Drosophila relies on the integration of chemical and mechanical signaling between the developing muscles with ectodermal cells specialized as "tendon cells." Mechanical tension generated at the junction of flight muscles and tendon cells of the notum epithelium is required for muscle morphogenesis, and is balanced by the epithelium in order to not deform. We report that Drosophila Rho kinase (DRok) is necessary in tendon cells to assemble stable myotendinous junctions (MTJ), which are required for muscle morphogenesis and survival. In addition, DRok is required in tendon cells to maintain epithelial shape and cell orientation in the notum, independently of chascon (chas). Loss of DRok function in tendon cells results in misorientation of tendon cell extensions and abnormal accumulation of Thrombospondin and bPS-integrin, which may cause abnormal myotendinous junction formation and muscle morphogenesis. This role does not depend exclusively on nonmuscular Myosin-II activation (Myo-II), indicating that other DRok targets are key in this process. We propose that DRok function in tendon cells is key to promote the establishment of MTJ attachment and to balance mechanical tension generated at the MTJ by muscle compaction.

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Simulation and in vivo experimentation predict AdamTS‐A location of function during caudal visceral mesoderm migration in Drosophila

Hamilton

Stolarska

Ismat

2022

Developmental Dynamics

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Background Caudal visceral mesoderm (CVM) cells migrate as a loose collective along the trunk visceral mesoderm (TVM) and are surrounded by extracellular matrix (ECM). In this study, we examined how one extracellular protease, AdamTS‐A, facilitates CVM migration. Results A comparison of mathematical simulation to experimental results suggests that location of AdamTS‐A action in CVM cells is on the sides of the cell not in contact with the TVM, predominantly at the CVM‐ECM interface. CVM migration from a top‐down view showed CVM cells migrating along the outside of the TVM substrate in the absence of AdamTS‐A. Moreover, overexpression of AdamTS‐A resulted in similar, but milder, mis‐migration of the CVM. These results contrast with the salivary gland where AdamTS‐A is proposed to cleave connections at the trailing edge of migrating cells. Subcellular localization of GFP‐tagged AdamTS‐A suggests that this protease is not limited to functioning at the trailing edge of CVM cells. Conclusion Using both in vivo experimentation and mathematical simulations, we demonstrated that AdamTS‐A cleaves connections between CVM cells and the ECM on all sides not attached to the TVM. Clearly, AdamTS‐A has a more expansive role around the entire cell in cleaving cell‐ECM attachments in cells migrating as a loose collective.

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The many faces of cell adhesion during Drosophila muscle development

Cited by 56 publications

References 175 publications

Kon-tiki enhances PS2 integrin adhesion and localizes its ligand, Thrombospondin, in the myotendinous junction

Kon-tiki enhances PS2 integrin adhesion and localizes its ligand, Thrombospondin, in the myotendinous junction

Establishment of the Muscle–Tendon Junction During Thorax Morphogenesis in Drosophila Requires the Rho-Kinase

Simulation and in vivo experimentation predict AdamTS‐A location of function during caudal visceral mesoderm migration in Drosophila

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