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A feedback mechanism converts individual cell features into a supracellular ECM structure in Drosophila trachea.

Öztürk-Çolak A, Moussian B, Araújo SJ, Casanova J - Elife (2016)

Bottom Line: Furthermore, we reveal that cell-cell junctions are key players in this aECM patterning and organisation and that individual cells contribute autonomously to their aECM.Strikingly, changes in the aECM influence the levels of phosphorylated Src42A (pSrc) at cell junctions.Therefore, we propose that Src42A phosphorylation levels provide a link for the ECM environment to ensure proper cytoskeletal organisation.

View Article: PubMed Central - PubMed

Affiliation: Institut de Biologia Molecular de Barcelona, Parc Cientific de Barcelona, Barcelona, Spain.

ABSTRACT
The extracellular matrix (ECM), a structure contributed to and commonly shared by many cells in an organism, plays an active role during morphogenesis. Here, we used the Drosophila tracheal system to study the complex relationship between the ECM and epithelial cells during development. We show that there is an active feedback mechanism between the apical ECM (aECM) and the apical F-actin in tracheal cells. Furthermore, we reveal that cell-cell junctions are key players in this aECM patterning and organisation and that individual cells contribute autonomously to their aECM. Strikingly, changes in the aECM influence the levels of phosphorylated Src42A (pSrc) at cell junctions. Therefore, we propose that Src42A phosphorylation levels provide a link for the ECM environment to ensure proper cytoskeletal organisation.

No MeSH data available.


Related in: MedlinePlus

Taenidial folds and F-actin rings in tal/pri, DAAM, and Btk29A mutants.Wild-type (A, B), tal/pri (C-D), DAAM (E-F), and Btk29A (G-H) mutant embryos stained with fluostain (A, C, E, G) to label taenidial folds and phalloidin (B, D, F, H) to label F-actin bundles. Both taenidial folds and F-actin bundles run perpendicular to the tube axis in wild-type embryos (A, B) while in most of the pri mutants they are parallel to the tube axis (C, D). In DAAM (E-F) and Btk29A (G-H) mutant embryos, taenidial folds and actin bundles are hardly detected and when so they appear mis-oriented, running both parallel and perpendicular to the tube axis. In all panels anterior is to the left and scale bars =10 μm.DOI:http://dx.doi.org/10.7554/eLife.09373.005
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fig2: Taenidial folds and F-actin rings in tal/pri, DAAM, and Btk29A mutants.Wild-type (A, B), tal/pri (C-D), DAAM (E-F), and Btk29A (G-H) mutant embryos stained with fluostain (A, C, E, G) to label taenidial folds and phalloidin (B, D, F, H) to label F-actin bundles. Both taenidial folds and F-actin bundles run perpendicular to the tube axis in wild-type embryos (A, B) while in most of the pri mutants they are parallel to the tube axis (C, D). In DAAM (E-F) and Btk29A (G-H) mutant embryos, taenidial folds and actin bundles are hardly detected and when so they appear mis-oriented, running both parallel and perpendicular to the tube axis. In all panels anterior is to the left and scale bars =10 μm.DOI:http://dx.doi.org/10.7554/eLife.09373.005

Mentions: Alteration of the tracheal apical F-bundles by mutants in genes encoding actin polymerisation proteins also cause defects in taenidial arrangement (Matusek et al., 2006). Such is the case for mutants for tarsal-less (tal), also known as polished rice (pri), a gene transcribed into a polycistronic mRNA that contains short ORFs encoding 11 or 32 amino acid-long peptides (Kondo et al., 2007; Galindo et al., 2007). Interestingly, tal/pri is essential for the formation of actin bundles that prefigure two chitin structures, namely denticles in the embryonic cuticle and taenidia in the trachea (Kondo et al., 2007). To further address the contribution of tracheal actin bundles to the arrangement of taenidia, we examined these two structures in the same mutant trachea to assess whether they are strictly correlated. In most tal/pri mutant embryos, the tracheal F-actin bundles formed but they were misoriented and did not follow the ring distribution found in the wild-type (Figure 2B,D); in some extreme cases, the bundles were completely disorganised. In all the cases studied, we found taenidia to be organised along the same pattern as the F-actin bundles, either running parallel to the tube axis when actin bundles were oriented in this way (Figure 2C), completely disorganised, or completely misshapen in twisted tracheal tubes when F-actin fibres were aligned in a twisted manner.10.7554/eLife.09373.005Figure 2.Taenidial folds and F-actin rings in tal/pri, DAAM, and Btk29A mutants.


A feedback mechanism converts individual cell features into a supracellular ECM structure in Drosophila trachea.

Öztürk-Çolak A, Moussian B, Araújo SJ, Casanova J - Elife (2016)

Taenidial folds and F-actin rings in tal/pri, DAAM, and Btk29A mutants.Wild-type (A, B), tal/pri (C-D), DAAM (E-F), and Btk29A (G-H) mutant embryos stained with fluostain (A, C, E, G) to label taenidial folds and phalloidin (B, D, F, H) to label F-actin bundles. Both taenidial folds and F-actin bundles run perpendicular to the tube axis in wild-type embryos (A, B) while in most of the pri mutants they are parallel to the tube axis (C, D). In DAAM (E-F) and Btk29A (G-H) mutant embryos, taenidial folds and actin bundles are hardly detected and when so they appear mis-oriented, running both parallel and perpendicular to the tube axis. In all panels anterior is to the left and scale bars =10 μm.DOI:http://dx.doi.org/10.7554/eLife.09373.005
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4764556&req=5

fig2: Taenidial folds and F-actin rings in tal/pri, DAAM, and Btk29A mutants.Wild-type (A, B), tal/pri (C-D), DAAM (E-F), and Btk29A (G-H) mutant embryos stained with fluostain (A, C, E, G) to label taenidial folds and phalloidin (B, D, F, H) to label F-actin bundles. Both taenidial folds and F-actin bundles run perpendicular to the tube axis in wild-type embryos (A, B) while in most of the pri mutants they are parallel to the tube axis (C, D). In DAAM (E-F) and Btk29A (G-H) mutant embryos, taenidial folds and actin bundles are hardly detected and when so they appear mis-oriented, running both parallel and perpendicular to the tube axis. In all panels anterior is to the left and scale bars =10 μm.DOI:http://dx.doi.org/10.7554/eLife.09373.005
Mentions: Alteration of the tracheal apical F-bundles by mutants in genes encoding actin polymerisation proteins also cause defects in taenidial arrangement (Matusek et al., 2006). Such is the case for mutants for tarsal-less (tal), also known as polished rice (pri), a gene transcribed into a polycistronic mRNA that contains short ORFs encoding 11 or 32 amino acid-long peptides (Kondo et al., 2007; Galindo et al., 2007). Interestingly, tal/pri is essential for the formation of actin bundles that prefigure two chitin structures, namely denticles in the embryonic cuticle and taenidia in the trachea (Kondo et al., 2007). To further address the contribution of tracheal actin bundles to the arrangement of taenidia, we examined these two structures in the same mutant trachea to assess whether they are strictly correlated. In most tal/pri mutant embryos, the tracheal F-actin bundles formed but they were misoriented and did not follow the ring distribution found in the wild-type (Figure 2B,D); in some extreme cases, the bundles were completely disorganised. In all the cases studied, we found taenidia to be organised along the same pattern as the F-actin bundles, either running parallel to the tube axis when actin bundles were oriented in this way (Figure 2C), completely disorganised, or completely misshapen in twisted tracheal tubes when F-actin fibres were aligned in a twisted manner.10.7554/eLife.09373.005Figure 2.Taenidial folds and F-actin rings in tal/pri, DAAM, and Btk29A mutants.

Bottom Line: Furthermore, we reveal that cell-cell junctions are key players in this aECM patterning and organisation and that individual cells contribute autonomously to their aECM.Strikingly, changes in the aECM influence the levels of phosphorylated Src42A (pSrc) at cell junctions.Therefore, we propose that Src42A phosphorylation levels provide a link for the ECM environment to ensure proper cytoskeletal organisation.

View Article: PubMed Central - PubMed

Affiliation: Institut de Biologia Molecular de Barcelona, Parc Cientific de Barcelona, Barcelona, Spain.

ABSTRACT
The extracellular matrix (ECM), a structure contributed to and commonly shared by many cells in an organism, plays an active role during morphogenesis. Here, we used the Drosophila tracheal system to study the complex relationship between the ECM and epithelial cells during development. We show that there is an active feedback mechanism between the apical ECM (aECM) and the apical F-actin in tracheal cells. Furthermore, we reveal that cell-cell junctions are key players in this aECM patterning and organisation and that individual cells contribute autonomously to their aECM. Strikingly, changes in the aECM influence the levels of phosphorylated Src42A (pSrc) at cell junctions. Therefore, we propose that Src42A phosphorylation levels provide a link for the ECM environment to ensure proper cytoskeletal organisation.

No MeSH data available.


Related in: MedlinePlus