scholarly journals Larval salivary gland chromosomes of Simulium (Simulium) eximium (Diptera : Simuliidae) from Java and Sumatra, Indonesia, with implication of sibling speciation

1996 ◽  
Vol 47 (2) ◽  
pp. 139-144
Author(s):  
Upik Kesumawati HADI ◽  
Hiroyuki TAKAOKA ◽  
Kashiko KONDO ◽  
Hirohisa HIRAI
Genetics ◽  
2000 ◽  
Vol 156 (1) ◽  
pp. 229-244
Author(s):  
Martina Vaskova ◽  
A M Bentley ◽  
Samantha Marshall ◽  
Pamela Reid ◽  
Carl S Thummel ◽  
...  

Abstract The 63F early puff in the larval salivary gland polytene chromosomes contains the divergently transcribed E63-1 and E63-2 ecdysone-inducible genes. E63-1 encodes a member of the EF-hand family of Ca2+-binding proteins, while E63-2 has no apparent open reading frame. To understand the functions of the E63 genes, we have determined the temporal and spatial patterns of E63-1 protein expression, as well as undertaken a genetic analysis of the 63F puff. We show that E63-1 is expressed in many embryonic and larval tissues, but the third-instar larval salivary gland is the only tissue where increases in protein levels correlate with increases in ecdysone titer. Furthermore, the subcellular distribution of E63-1 protein changes dynamically in the salivary glands at the onset of metamorphosis. E63-1 and E63-2 null mutations, however, have no effect on development or fertility. We have characterized 40 kb of the 63F region, defined as the interval between Ubi-p and E63-2, and have identified three lethal complementation groups that correspond to the dSc-2, ida, and mge genes. We show that mge mutations lead to first-instar larval lethality and that Mge protein is similar to the Tom22 mitochondrial import proteins of fungi, suggesting that it has a role in mitochondrial function.


1971 ◽  
Vol 49 (1) ◽  
pp. 132-133 ◽  
Author(s):  
Albert E. Moorman

Acetic-acid-fixed smears of Drosophila larval salivary gland chromosomes and of neuroblast cells from the larval ganglion undergoing mitosis are prepared by a modification of Heidenhain's iron-haematoxylin technique, in which absolute methyl alcohol is the solvent of all reagents used in the staining process.


1988 ◽  
Vol 8 (5) ◽  
pp. 1877-1886
Author(s):  
B M Benton ◽  
S Berrios ◽  
P A Fisher

A 75-kilodalton polypeptide has been identified which copurifies with karyoskeletal protein-enriched fractions prepared from Drosophila melanogaster embryos. Results of indirect immunofluorescence experiments suggest that this protein, here designated p75, is primarily associated with puffed regions of larval salivary gland polytene chromosomes. In nonpolytenized Schneider 2 tissue culture cells, p75 appeared to be localized throughout the nuclear interior during interphase. In mitotic cells, p75 was redistributed diffusely. A possible role for karyoskeletal elements in transcriptional regulation is discussed.


1984 ◽  
Vol 179 (3) ◽  
pp. 289-314 ◽  
Author(s):  
Gregory M. Guild ◽  
Eileen Malko Shore

1991 ◽  
Vol 207 (1) ◽  
pp. 17-21 ◽  
Author(s):  
George N. Thomopoulos ◽  
Elefterios P. Neophytou ◽  
Stella Limberi-Thomopoulos

2019 ◽  
Author(s):  
Johanna Lattner ◽  
Weihua Leng ◽  
Elisabeth Knust ◽  
Marko Brankatschk ◽  
David Flores-Benitez

AbstractAn efficient vectorial intracellular transport machinery depends on a well-established apico-basal polarity and is a prerequisite for the function of secretory epithelia. Despite extensive knowledge on individual trafficking pathways, little is known about the mechanisms coordinating their temporal and spatial regulation. Here, we report that the polarity protein Crumbs is essential for apical plasma membrane phospholipid-homeostasis and efficient apical secretion. Through recruiting βHeavy-Spectrin and MyosinV to the apical membrane, Crumbs maintains the Rab6-, Rab11- and Rab30-dependent trafficking and regulates the lipid phosphatases Pten and Ocrl. Crumbs knock-down results in increased apical levels of PI(4,5)P2 and formation of a novel, Moesin- and PI(4,5)P2-enriched apical membrane sac containing microvilli-like structures. Our results identify Crumbs as an essential hub required to maintain the organization of the apical membrane and the physiological activity of the larval salivary gland.


Cells ◽  
2018 ◽  
Vol 7 (10) ◽  
pp. 151 ◽  
Author(s):  
Yifat Yanku ◽  
Eliya Bitman-Lotan ◽  
Yaniv Zohar ◽  
Estee Kurant ◽  
Norman Zilke ◽  
...  

The HECT-type ubiquitin ligase HECT, UBA and WWE Domain Containing 1, (HUWE1) regulates key cancer-related pathways, including the Myc oncogene. It affects cell proliferation, stress and immune signaling, mitochondria homeostasis, and cell death. HUWE1 is evolutionarily conserved from Caenorhabditis elegance to Drosophila melanogaster and Humans. Here, we report that the Drosophila ortholog, dHUWE1 (CG8184), is an essential gene whose loss results in embryonic lethality and whose tissue-specific disruption establishes its regulatory role in larval salivary gland development. dHUWE1 is essential for endoreplication of salivary gland cells and its knockdown results in the inability of these cells to replicate DNA. Remarkably, dHUWE1 is a survival factor that prevents premature activation of JNK signaling, thus preventing the disintegration of the salivary gland, which occurs physiologically during pupal stages. This function of dHUWE1 is general, as its inhibitory effect is observed also during eye development and at the organismal level. Epistatic studies revealed that the loss of dHUWE1 is compensated by dMyc proeitn expression or the loss of dmP53. dHUWE1 is therefore a conserved survival factor that regulates organ formation during Drosophila development.


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