Differential localization and processing of apoptotic proteins in Malpighian tubules of Drosophila during metamorphosis

Shukla, Anukampa; Tapadia, Madhu G.

doi:10.1016/j.ejcb.2010.08.010

Cited by 17 publications

(26 citation statements)

References 49 publications

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“…The nuclei were counterstained with DAPI (figure 2B, E, H, K) and the merged images show that these proteins localize predominantly to the cytoplasm with little or no expression in the nucleus (figure 2C, F, I, L). This is in contrast to our earlier report that the localization of apoptotic protein in the 3rd larval and pupal MTs is predominantly nuclear (Shukla and Tapadia 2011). These data suggest that the expression of apoptotic genes hid and grim, but not rpr, commences from early development of the MTs during embryogenesis and continues into the larval stages.…”

Section: Expression Of Pro-apoptotic Proteins In Mts During Early Devcontrasting

confidence: 86%

“…In the present results we show that disturbing the levels of apoptotic proteins affects the distribution pattern of cytoskeletal proteins and Dlg. In our previous report we have shown that the apoptotic proteins are also present on the basal membrane of MTs apart from the nucleus (Shukla and Tapadia 2011), and it could be possible that these apoptotic proteins could play a scaffolding role in maintaining the integrity of epithelial structures. Whether apoptotic proteins have a direct function in regulating the cytoskeletal elements and other membrane protein complexes and, in turn, controlling the organization is still to be understood.…”

Section: Discussionmentioning

confidence: 99%

“…The expression of pro-apoptotic genes, rpr, hid and grim and their ectopic expression leading to activation of caspases and apoptosis, is well correlated with cell death (Song et al 2000). In our recent report (Shukla and Tapadia 2011) we have shown that these proteins also express and show nuclear localization in the 3rd instar larval and pupal MTs, which are tissues that do not undergo apoptosis during metamorphosis like other larval structures. To further investigate the expression of rpr, hid and grim in MTs at embryonic and 1st instar larval stages, MTs were immunostained with anti- Rpr show the co-localization of these proteins, demonstrating that the apoptotic genes do indeed express in MTs.…”

Section: Expression Of Pro-apoptotic Proteins In Mts During Early Devmentioning

confidence: 96%

“…Unlike most of larval tissues, which are histolysed during metamorphosis, MTs escape this fate and continue in the adult fly. Recent studies have shown that the different genes involved in apoptosis are expressed in the MTs but the proteins remain sequestered in the nucleus and are inhibited from being activated, thus allowing MTs to escape destruction (Shukla and Tapadia 2011).…”

Section: Introductionmentioning

confidence: 99%

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Non-apoptotic function of apoptotic proteins in the development of Malpighian tubules of Drosophila melanogaster

Tapadia

Gautam

2011

J Biosci

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Drosophila metamorphosis is characterized by the histolysis of larval structures by programmed cell death, which paves the way for the establishment of adult-specific structures under the influence of the steroid hormone ecdysone. Malpighian tubules function as an excretory system and are one of the larval structures that are not destroyed during metamorphosis and are carried over to adulthood. The pupal Malpighian tubules evade destruction in spite of expressing apoptotic proteins, Reaper, Hid, Grim, Dronc and Drice. Here we show that in the Malpighian tubules expression of apoptotic proteins commences right from embryonic development and continues throughout the larval stages. Overexpression of these proteins in the Malpighian tubules causes larval lethality resulting in malformed tubules. The number and regular organization of principal and stellate cells of Malpighian tubules is disturbed, in turn disrupting the physiological functioning of the tubules as well. Strikingly, the localization of beta-tubulin, F-actin and Disclarge (Dlg) is also disrupted. These results suggest that the apoptotic proteins could be having non-apoptotic function in the development of Malpighian tubules.

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Section: Expression Of Pro-apoptotic Proteins In Mts During Early Devcontrasting

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Expression Of Pro-apoptotic Proteins In Mts During Early Devmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Non-apoptotic function of apoptotic proteins in the development of Malpighian tubules of Drosophila melanogaster

Tapadia

Gautam

2011

J Biosci

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“…However, there are examples in which spatiotemporal control of caspase activity is required to induce differentiation while preventing cell death. For example, caspases play important roles in spermatid individualization (54,55), and Grim is expressed in Malpighian tubules during metamorphosis, implying that it plays a role in the formation of these tubules, but its expression is largely restricted to the nucleus (56,57). Thus, the interplay among DIAP1, caspases, Grim, and the proteasome may constitute a unique form of rheostatic control, such that, at relatively low levels of Grim, DIAP1 may allow for some caspase activity while limiting through ubiquitinylation the overall levels of Grim and active caspases.…”

Section: Discussionmentioning

confidence: 99%

Caspase-dependent regulation of the ubiquitin–proteasome system through direct substrate targeting

Yeh¹,

Bratton²

2013

Proc. Natl. Acad. Sci. U.S.A.

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Drosophila inhibitor of apoptosis (IAP) 1 (DIAP1) is an E3 ubiquitin ligase that regulates apoptosis in flies, in large part through direct inhibition and/or ubiquitinylation of caspases. IAP antagonists, such as Reaper, Hid, and Grim, are thought to induce cell death by displacing active caspases from baculovirus IAP repeat domains in DIAP1, but can themselves become targets of DIAP1-mediated ubiquitinylation. Herein, we demonstrate that Grim self-associates in cells and is ubiquitinylated by DIAP1 at Lys136 in an UbcD1-dependent manner, resulting in its rapid turnover. K48-linked ubiquitin chains are added almost exclusively to BIR2-bound Grim as a result of its structural proximity to DIAP1's RING domain. However, active caspases can simultaneously cleave Grim at Asp132, removing the lysine necessary for ubiquitinylation as well as any existing ubiquitin conjugates. Cleavage therefore enhances the stability of Grim and initiates a feed-forward caspase amplification loop, resulting in greater cell death. In summary, Grim is a caspase substrate whose cleavage promotes apoptosis by limiting, in a target-specific fashion, its ubiquitinylation and turnover by the proteasome.

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Nonapoptotic role of caspase‐3 in regulating Rho1GTPase‐mediated morphogenesis of epithelial tubes of Drosophila renal system

Ojha

Tapadia

2021

Developmental Dynamics

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Background: Cells trigger caspase-mediated apoptosis to eliminate themselves from the system when tissue needs to be sculptured, or they detect any abnormality within them, thus preventing irreparable damage to the host. However, nonapoptotic activities of caspases are also involved in many cellular functions. Interestingly, Drosophila Malpighian tubules (MTs) express apoptotic proteins, without succumbing to cell death.Results: We show apoptosis-independent role of executioner caspase-3, Drice, in MT morphogenesis. Drice is required for precise cytoskeleton organization and convergent extension, failing which morphology, size, cell number, and arrangement get affected. Furthermore, characteristic stellate cell shape transformation in MTs is also governed by Drice. Genetic interaction study shows that Drice mediates its action by regulating Rho1GTPase functionally, and localization of polarity protein Disc large. Subsequently, downregulation of Rho1GTPase in Drice mutants significantly rescues the cystic MTs phenotype.The study shows a mechanism by which Drice governs tubulogenesis via Rho1GTPase-mediated coordinated organization of actin cytoskeleton and membrane stabilization. Conclusion: Collectively our findings suggest a nonapoptotic function of caspase-3 in fine-tuning of cellular rearrangement during tubule development, and these results will add to the growing understanding of diverse roles of caspases during its evolution in metazoans.

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Differential localization and processing of apoptotic proteins in Malpighian tubules of Drosophila during metamorphosis

Cited by 17 publications

References 49 publications

Non-apoptotic function of apoptotic proteins in the development of Malpighian tubules of Drosophila melanogaster

Non-apoptotic function of apoptotic proteins in the development of Malpighian tubules of Drosophila melanogaster

Caspase-dependent regulation of the ubiquitin–proteasome system through direct substrate targeting

Nonapoptotic role of caspase‐3 in regulating Rho1GTPase‐mediated morphogenesis of epithelial tubes of Drosophila renal system

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