scholarly journals Feedback inhibition of actin on Rho mediates content release from large secretory vesicles

2018 ◽  
Vol 217 (5) ◽  
pp. 1815-1826 ◽  
Author(s):  
Dagan Segal ◽  
Assaf Zaritsky ◽  
Eyal D. Schejter ◽  
Ben-Zion Shilo
Keyword(s):  
Drosophila Melanogaster ◽  
Salivary Glands ◽  
Negative Feedback ◽  
Temporal Order ◽  
Feedback Inhibition ◽  
Secretory Vesicles ◽  
Actin Turnover ◽  
Apical Membranes ◽  
Contraction Cycle ◽  
Actomyosin Contraction

Secretion of adhesive glycoproteins to the lumen of Drosophila melanogaster larval salivary glands is performed by contraction of an actomyosin network assembled around large secretory vesicles, after their fusion to the apical membranes. We have identified a cycle of actin coat nucleation and disassembly that is independent of myosin. Recruitment of active Rho1 to the fused vesicle triggers activation of the formin Diaphanous and actin nucleation. This leads to actin-dependent localization of a RhoGAP protein that locally shuts off Rho1, promoting disassembly of the actin coat. When contraction of vesicles is blocked, the strict temporal order of the recruited elements generates repeated oscillations of actin coat formation and disassembly. Interestingly, different blocks to actin coat disassembly arrested vesicle contraction, indicating that actin turnover is an integral part of the actomyosin contraction cycle. The capacity of F-actin to trigger a negative feedback on its own production may be widely used to coordinate a succession of morphogenetic events or maintain homeostasis.

scholarly journals Formation and disassembly of a contractile actomyosin network mediates content release from large secretory vesicles

2017 ◽  
Author(s):  
Dagan Segal ◽  
Assaf Zaritsky ◽  
Eyal D. Schejter ◽  
Ben-Zion Shilo
Keyword(s):  
Salivary Glands ◽  
Negative Feedback ◽  
Secretory Vesicles ◽  
Actin Assembly ◽  
Actin Nucleation ◽  
Actin Turnover ◽  
Apical Membranes ◽  
Contraction Cycle ◽  
Actomyosin Contraction

AbstractSecretion of adhesive glycoproteins to the lumen of Drosophila larval salivary glands is carried out by contraction of an actomyosin network that is assembled around large secretory vesicles, following their fusion to the apical membranes. We have identified a cycle of actin coat nucleation and disassembly that is independent of myosin. Recruitment of active Rho1 to the fused vesicle triggers activation of the formin Diaphanous and nucleation of linear actin. This, in turn, leads to actin-dependent localization of a RhoGAP protein that locally shuts off Rho1, promoting disassembly of the actin coat. Recruitment of the branched actin nucleation machinery is also required for effective Rho1 inactivation. Interestingly, different blocks to actin coat disassembly arrested vesicle contraction, indicating that actin turnover is an integral part of the actomyosin contraction cycle. The capacity of F-actin to trigger a negative feedback on its own production may be utilized in a variety of scenarios, to coordinate a succession of morphogenetic events or maintain homeostasis.SummaryThis work identified a cycle of actin assembly and disassembly in large secretory vesicles of Drosophila salivary glands. Actin disassembly is triggered by actin-dependent recruitment of a RhoGAP protein, and is essential for the contractility of the vesicle leading to content release to the lumen.

Ultrastructural Analysis of the Salivary Glands of Gromphadorhina Portentosa (Schaum)

1977 ◽  
Vol 35 ◽  
pp. 638-639
Author(s):  
P.J. Dailey
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Salivary Glands ◽  
Secretory Vesicles ◽  
The Past ◽  
Transmission Electron ◽  
Means Of Transmission ◽  
Gromphadorhina Portentosa ◽  
Scanning Electron ◽  
Topographical Relief

The structure of insect salivary glands has been extensively investigated during the past decade; however, none have attempted scanning electron microscopy (SEM) in ultrastructural examinations of these secretory organs. This study correlates fine structure by means of SEM cryofractography with that of thin-sectioned epoxy embedded material observed by means of transmission electron microscopy (TEM).Salivary glands of Gromphadorhina portentosa were excised and immediately submerged in cold (4°C) paraformaldehyde-glutaraldehyde fixative1 for 2 hr, washed and post-fixed in 1 per cent 0s04 in phosphosphate buffer (4°C for 2 hr). After ethanolic dehydration half of the samples were embedded in Epon 812 for TEM and half cryofractured and subsequently critical point dried for SEM. Dried specimens were mounted on aluminum stubs and coated with approximately 150 Å of gold in a cold sputtering apparatus.Figure 1 shows a cryofractured plane through a salivary acinus revealing topographical relief of secretory vesicles.

Studies on Nucleolar RNA Synthesis in Drosophila Melanogaster

1972 ◽  
Vol 11 (3) ◽  
pp. 689-697
Author(s):  
H. M. KRIDER ◽  
W. PLAUT
Keyword(s):  
Drosophila Melanogaster ◽  
Salivary Glands ◽  
Rna Synthesis ◽  
First Generation ◽  
Nucleolus Organizer ◽  
Fifth Generation ◽  
Autoradiographic Analysis ◽  
Temporally Correlated ◽  
Nucleolar Rna ◽  
Nucleolus Organizers

The influence of conditions resulting in bobbed phenotypes on nucleolar RNA synthesis and the formation of constrictions at nucleolus organizers was examined in larval tissues of Drosophila melanogaster. By means of [3H]uridine incorporation and autoradiographic analysis, a mutation at the bobbed locus was shown to limit the rate of nucleolar RNA synthesis in salivary glands of XO larvae. The formation of constrictions at the organizer sites of a 4-nucleolus-organizer stock was monitored in dividing neuroblast cells stained with acridine orange. Loss of the ribosomal cistrons had been reported by other workers when such stocks were maintained for several generations. In the first generation in our work, constrictions were visible at only 2 of the 4 nucleolus organizers. This situation persisted until the fifth generation, when constrictions appeared at all 4 of the organizer sites. An increase in the rate of nucleolar RNA synthesis in the salivary glands was temporally correlated with the appearance of the extra constrictions. We interpret these observations to mean that 2 of the organizers of the 4-nucleolus-organizer stock were caused to function through the loss of ribosomal RNA cistrons; thus the functional status of an organizer would appear to be subject to control.

2. Negative feedback inhibition – Fundamental biological regulation in cells and organisms

2015 ◽  
Author(s):  
Jakub Wach ◽  
Marian Bubak ◽  
Piotr Nowakowski ◽  
Irena Roterman ◽  
Leszek Konieczny ◽  
...  
Keyword(s):  
Negative Feedback ◽  
Feedback Inhibition ◽  
Biological Regulation ◽  
In Cells

Role of facilitated diffusion of calcium by calbindin in intestinal calcium absorption

1992 ◽  
Vol 262 (2) ◽  
pp. C517-C526 ◽  
Author(s):  
J. J. Feher ◽  
C. S. Fullmer ◽  
R. H. Wasserman
Keyword(s):  
Negative Feedback ◽  
Calcium Absorption ◽  
Feedback Inhibition ◽  
Basolateral Membrane ◽  
Reaction Diffusion ◽  
Diffusion Problem ◽  
Facilitated Diffusion ◽  
Calbindin D9k ◽  
And Diffusion

Computer simulations of transcellular Ca2+ transport in enterocytes were carried out using the simulation program SPICE. The program incorporated a negative-feedback entry of Ca2+ at the brush-border membrane that was characterized by an inhibitor constant of 0.5 microM cytosolic Ca2+ concentration ([Ca2+]). The basolateral Ca(2+)-ATPase was simulated by a four-step mechanism that resulted in Michaelis-Menten kinetics with a Michaelis constant of 0.24 microM [Ca2+]. The cytosolic diffusion of Ca2+ was simulated by dividing the cytosol into 10 slabs of equal width. Ca2+ binding to calbindin-D9K was simulated in each slab, and diffusion of free Ca2+, free calbindin, and Ca(2+)-laden calbindin was simulated between each slab. The cytosolic [Ca2+] of the simulated cells was regulated within the physiological range. Calbindin-D9K reduced the cytosolic [Ca2+] gradient, increased Ca2+ entry into the cell by removing the negative-feedback inhibition of Ca2+ entry, increased cytosolic Ca2+ flow, and increased the efflux of Ca2+ across the basolateral membrane by increasing the free [Ca2+] immediately adjacent to the pump. The enhancement of transcellular Ca2+ transport was nearly linearly dependent on calbindin-D9K concentration. The values of the dissociation constant (Kd) for calbindin-D9K were previously obtained experimentally in the presence and absence of KCl. Calbindin with the Kd obtained in the presence of KCl enhanced the simulated Ca2+ transport more than with the Kd obtained in the absence of KCl. This result suggests that the physiological Kd of calbindin is optimal for the enhancement of transcellular Ca2+ transport. The simulated Ca2+ flow was less than that predicted from the "near-equilibrium" analytic solution of the reaction-diffusion problem.

20-OH-ecdysone swells nuclear volume by alkalinization in salivary glands of Drosophila melanogaster

1993 ◽  
Vol 274 (1) ◽  
pp. 145-151 ◽  
Author(s):  
Stefan W�nsch ◽  
Stefan Schneider ◽  
Albrecht Schwab ◽  
Hans Oberleithner
Keyword(s):  
Drosophila Melanogaster ◽  
Salivary Glands ◽  
Nuclear Volume
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