Identification of vitelline membrane proteins in Drosophila melanogaster

1982 ◽  
Vol 92 (2) ◽  
pp. 306-314 ◽  
Author(s):  
Joseph Fargnoli ◽  
Gail L. Waring
1993 ◽  
Vol 155 (2) ◽  
pp. 558-568 ◽  
Author(s):  
Yonggu Lin ◽  
Martha T. Hamblin ◽  
Marten J. Edwards ◽  
Carolina Barillas-Mury ◽  
Michael R. Kanost ◽  
...  

Gene ◽  
1993 ◽  
Vol 136 (1-2) ◽  
pp. 121-127 ◽  
Author(s):  
L.J. Scherer ◽  
D.H. Harris ◽  
M.K. White ◽  
L.F. Steel ◽  
J. Jin ◽  
...  

1998 ◽  
Vol 206 (5) ◽  
pp. 329-332 ◽  
Author(s):  
Annette Schäfer ◽  
Wiebke Drewes ◽  
F. Schwägele

2006 ◽  
Vol 173 (1) ◽  
pp. 69-82 ◽  
Author(s):  
Usha Acharya ◽  
Michael Beth Edwards ◽  
Ramon A. Jorquera ◽  
Hugo Silva ◽  
Kunio Nagashima ◽  
...  

Scramblases are a family of single-pass plasma membrane proteins, identified by their purported ability to scramble phospholipids across the two layers of plasma membrane isolated from platelets and red blood cells. However, their true in vivo role has yet to be elucidated. We report the generation and isolation of null mutants of two Scramblases identified in Drosophila melanogaster. We demonstrate that flies lacking either or both of these Scramblases are not compromised in vivo in processes requiring scrambling of phospholipids. Instead, we show that D. melanogaster lacking both Scramblases have more vesicles and display enhanced recruitment from a reserve pool of vesicles and increased neurotransmitter secretion at the larval neuromuscular synapses. These defects are corrected by the introduction of a genomic copy of the Scramb 1 gene. The lack of phenotypes related to failure of scrambling and the neurophysiological analysis lead us to propose that Scramblases play a modulatory role in the process of neurotransmission.


2019 ◽  
Vol 449 (1) ◽  
pp. 52-61 ◽  
Author(s):  
Yuka Tanaka ◽  
Shiori Yamada ◽  
Samantha L. Connop ◽  
Noritaka Hashii ◽  
Hitoshi Sawada ◽  
...  

1980 ◽  
Vol 43 (1) ◽  
pp. 1-35 ◽  
Author(s):  
L.H. Margaritis ◽  
F.C. Kafatos ◽  
W.H. Petri

The fine structure of the several layers and regional specializations in the Drosophila melanogaster eggshell has been studied by a combination of shell isolation procedures and ultrastructural techniques (conventional TEM, whole-mount TEM, SEM, HVEM, freeze-fracture electron microscopy utilizing rotary replication, shadow casting, optical diffraction and stereo imaging). The main shell consists of 5 layers: the vitelline membrane (300 nm thick), the wax layer, the innermost chorionic layer (40-50 nm), the endochorion (500-700 nm), and the exochorion (300-500 nm). The vitelline membrane consists of irregularly organized particles. The wax layer appears to contain multilayered hydrophobic plates which split tangenitally upon freeze fracturing. The innermost chorionic layer is composed of a crystalling lattice. The endochorion is made of a thin (40 nm) fenestrated floor composed of 40-nm fibres and an outer solid (200 nm) roof covered with a network of 40-nm strands. Intermittently spaced pillar connect these 2 parts. Similarities in the substructure of the floor, pillars and roof suggest that they may be composed of similar or identical structural elements. The specialized regions of the shell are the 2 respiratory appendages, the operculum area and the posterior pole. The appendages exhibit 2 sharply distinct surfaces, a dorsal side with isolated 1.5-micrometer plaques and a ventral side with strands of 40–50 nm connected in a network with openings of 70–80 nm. The operculum area, which includes the micropoyle and the collar, is distinguished by 3 unique types of cell imprints. The posterior pole contains 2 distinctive populations of cell imprints: the central area has very thin intercellular ridges and a thin, perforated, endochorionic roof, while the peripheral area contains mixed, thick and thin, intercellular ridges and serves as a transition zone to the main shell pattern. The pillars in the central area of the posterior pole have a distinct arrangement, forming one peripheral circle within each cell imprint. An analysis utilizing structural and developmental criteria indicates that as many as ten different populations of follicular epithelial cells may be involved in the construction of the various regions of the Drosophila eggshell.


2007 ◽  
Vol 292 (3) ◽  
pp. C1132-C1136 ◽  
Author(s):  
Alexandre Leduc-Nadeau ◽  
Karim Lahjouji ◽  
Pierre Bissonnette ◽  
Jean-Yves Lapointe ◽  
Daniel G. Bichet

Over the past two decades, Xenopus laevis oocytes have been widely used as an expression system to investigate both physiological and pathological properties of membrane proteins such as channels and transporters. Past studies have clearly shown the key implications of mistargeting in relation to the pathogenesis of these proteins. To unambiguously determine the plasma membrane targeting of a protein, a thorough purification technique becomes essential. Unfortunately, available techniques are either too cumbersome, technically demanding, or require large amounts of material, all of which are not adequate when using oocytes individually injected with cRNA or DNA. In this article, we present a new technique that permits excellent purification of plasma membranes from X. laevis oocytes. This technique is fast, does not require particular skills such as peeling of vitelline membrane, and permits purification of multiple samples from as few as 10 and up to >100 oocytes. The procedure combines partial digestion of the vitelline membrane, polymerization of the plasma membrane, and low-speed centrifugations. We have validated this technique essentially with Western blot assays on three plasma membrane proteins [aquaporin (AQP)2, Na+-glucose cotransporter (SGLT)1, and transient receptor potential vanilloid (TRPV)5], using both wild-type and mistargeted forms of the proteins. Purified plasma membrane fractions were easily collected, and samples were found to be adequate for Western blot identification.


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