Faculty Opinions recommendation of Gatekeeper function for Short stop at the ring canals of the Drosophila ovary.

2021 ◽  
Author(s):  
Beat Suter
Keyword(s):  
Ring Canals ◽  
Drosophila Ovary

Gatekeeper function for Short stop at the ring canals of the Drosophila ovary

2021 ◽  
Author(s):  
Wen Lu ◽  
Margot Lakonishok ◽  
Vladimir I. Gelfand
Keyword(s):  
Ring Canals ◽  
Drosophila Ovary

scholarly journals Short stop is a gatekeeper at the ring canals of Drosophila ovary

2020 ◽  
Author(s):  
Wen Lu ◽  
Margot Lakonishok ◽  
Vladimir I. Gelfand
Keyword(s):  
Actin Filaments ◽  
Cytoskeletal Proteins ◽  
Nurse Cells ◽  
Cellular Functions ◽  
Oocyte Growth ◽  
Ring Canals ◽  
Cytoplasmic Bridges ◽  
Drosophila Ovary ◽  
Open Nature ◽  
Sister Cells

SUMMARYMicrotubules and actin filaments are two major cytoskeletal components essential for a variety of cellular functions. Spectraplakins are a family of large cytoskeletal proteins cross-linking microtubules and actin filaments among other components. In this study, we aim to understand how Short stop (Shot), the single Drosophila spectraplakin, coordinates microtubules and actin filaments for oocyte growth. The oocyte growth completely relies on the acquisition of cytoplasmic materials from the interconnected sister cells (nurse cells), through ring canals, cytoplasmic bridges that remained open after incomplete germ cell division. Given the open nature of the ring canals, it is unclear how the direction of transport through the ring canal is controlled. Here we show that Shot controls the directionality of flow of material from the nurse cells towards the oocyte. Knockdown of shot changes the direction of transport of many types of cargo through the ring canals from unidirectional (toward the oocyte) to bidirectional, resulting in small oocytes that fail to grow over time. In agreement with this flow-directing function of Shot, we find that it is localized at the asymmetric actin fibers adjacent to the ring canals at the nurse cell side, and controls the uniform polarity of microtubules located in the ring canals connecting the nurse cells and the oocyte. Together, we propose that Shot functions as a gatekeeper directing the material flow from the nurse cells to the oocyte, via organization of microtubule tracks.

scholarly journals A novel mechanism of bulk cytoplasmic transport by cortical dynein in Drosophila ovary

2021 ◽  
Author(s):  
Wen Lu ◽  
Margot Lakonishok ◽  
Anna S. Serpinskaya ◽  
Vladimir I Gelfand
Keyword(s):  
Cytoplasmic Dynein ◽  
Cell Cortex ◽  
Nurse Cells ◽  
Oocyte Growth ◽  
Actin Cortex ◽  
Cytoplasmic Transport ◽  
Ring Canals ◽  
Microtubule Motor ◽  
Cytoplasmic Bridges ◽  
Drosophila Ovary

Cytoplasmic dynein, a major minus-end directed microtubule motor, plays essential roles in eukaryotic cells. Drosophila oocyte growth is mainly dependent on the contribution of cytoplasmic contents from the interconnected sister cells, nurse cells. We have previously shown that cytoplasmic dynein is required for Drosophila oocyte growth, and assumed that it transports cargoes along microtubule tracks from nurse cells to the oocyte. Here we report that instead transporting cargoes along microtubules into the oocyte, cortical dynein actively moves microtubules in nurse cells and from nurse cells to the oocyte via the cytoplasmic bridges, the ring canals. We demonstrate this microtubule movement is sufficient to drag even inert cytoplasmic particles through the ring canals to the oocyte. Furthermore, replacing dynein with a minus-end directed plant kinesin linked to the actin cortex is sufficient for transporting organelles and cytoplasm to the oocyte and driving its growth. These experiments show that cortical dynein can perform bulk cytoplasmic transport by gliding microtubules along the cell cortex and through the ring canals to the oocyte. We propose that the dynein-driven microtubule flow could serve as a novel mode of cargo transport for fast cytoplasmic transfer to support rapid oocyte growth.  

Short Stop is a Gatekeeper at the Ring Canals of Drosophila Ovary

2020 ◽  
Author(s):  
Wen Lu ◽  
Margot Lakonishok ◽  
Vladimir I. Gelfand
Keyword(s):  
Ring Canals

scholarly journals Modulation of Cell–Cell Interactions in Drosophila Oocyte Development

Cells ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 274
Author(s):  
Matthew Antel ◽  
Mayu Inaba
Keyword(s):  
Cell Communication ◽  
Cell Interaction ◽  
Oocyte Development ◽  
Suitable Model ◽  
Physiological Regulation ◽  
Temporal Regulation ◽  
Cellular Processes ◽  
Cellular Machinery ◽  
Drosophila Ovary ◽  
Cell Cell

The Drosophila ovary offers a suitable model system to study the mechanisms that orchestrate diverse cellular processes. Oogenesis starts from asymmetric stem cell division, proper differentiation and the production of fully patterned oocytes equipped with all the maternal information required for embryogenesis. Spatial and temporal regulation of cell-cell interaction is particularly important to fulfill accurate biological outcomes at each step of oocyte development. Progress has been made in understanding diverse cell physiological regulation of signaling. Here we review the roles of specialized cellular machinery in cell-cell communication in different stages of oogenesis.

scholarly journals Dose-dependent modulation of HIF-1α/sima controls the rate of cell migration and invasion in Drosophila ovary border cells

Oncogene ◽  
2009 ◽  
Vol 29 (8) ◽  
pp. 1123-1134 ◽  
Author(s):  
S Doronkin ◽  
I Djagaeva ◽  
M E Nagle ◽  
L T Reiter ◽  
T N Seagroves
Keyword(s):  
Cell Migration ◽  
Migration And Invasion ◽  
Border Cells ◽  
Cell Migration And Invasion ◽  
Drosophila Ovary ◽  
Dose Dependent

Ectopic CRYPTOCHROME Renders TIM Light Sensitive in the Drosophila Ovary

2006 ◽  
Vol 21 (4) ◽  
pp. 272-278 ◽  
Author(s):  
Brandy L. Rush ◽  
Alejandro Murad ◽  
Patrick Emery ◽  
Jadwiga M. Giebultowicz
Keyword(s):  
Drosophila Ovary

scholarly journals Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm.

1995 ◽  
Vol 128 (1) ◽  
pp. 51-60 ◽  
Author(s):  
M Way ◽  
M Sanders ◽  
C Garcia ◽  
J Sakai ◽  
P Matsudaira
Keyword(s):  
Amino Acid ◽  
Actin Filaments ◽  
Limited Proteolysis ◽  
Open Reading Frames ◽  
Actin Binding ◽  
Molar Ratio ◽  
Domain Organization ◽  
Ring Canals ◽  
Drosophila Protein ◽  
Reading Frames

The acrosomal process of Limulus sperm is an 80-microns long finger of membrane supported by a crystalline bundle of actin filaments. The filaments in this bundle are crosslinked by a 102-kD protein, scruin present in a 1:1 molar ratio with actin. Recent image reconstruction of scruin decorated actin filaments at 13-A resolution shows that scruin is organized into two equally sized domains bound to separate actin subunits in the same filament. We have cloned and sequenced the gene for scruin from a Limulus testes cDNA library. The deduced amino acid sequence of scruin reflects the domain organization of scruin: it consists of a tandem pair of homologous domains joined by a linker region. The domain organization of scruin is confirmed by limited proteolysis of the purified acrosomal process. Three different proteases cleave the native protein in a 5-kD Protease-sensitive region in the middle of the molecule to generate an NH2-terminal 47-kD and a COOH-terminal 56-kD protease-resistant domains. Although the protein sequence of scruin has no homology to any known actin-binding protein, it has similarities to several proteins, including four open reading frames of unknown function in poxviruses, as well as kelch, a Drosophila protein localized to actin-rich ring canals. All proteins that show homologies to scruin are characterized by the presence of an approximately 50-amino acid residue motif that is repeated between two and seven times. Crystallographic studies reveal this motif represents a four beta-stranded fold that is characteristic of the "superbarrel" structural fold found in the sialidase family of proteins. These results suggest that the two domains of scruin seen in EM reconstructions are superbarrel folds, and they present the possibility that other members of this family may also bind actin.

Sign in / Sign up

Export Citation Format

Share Document