scholarly journals Endomembrane architecture and dynamics during secretion of the extracellular matrix of the unicellular charophyte, Penium margaritaceum

2020 ◽  
Vol 71 (11) ◽  
pp. 3323-3339 ◽  
Author(s):  
David S Domozych ◽  
Li Sun ◽  
Kattia Palacio-Lopez ◽  
Reagan Reed ◽  
Susan Jeon ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Brefeldin A ◽  
Extracellular Polysaccharide ◽  
Sister Group ◽  
Golgi Body ◽  
Endomembrane System ◽  
Golgi Bodies ◽  
Cytoplasmic Vesicles ◽  
Structural Details ◽  
Colonization Of Land

Abstract The extracellular matrix (ECM) of many charophytes, the assemblage of green algae that are the sister group to land plants, is complex, produced in large amounts, and has multiple essential functions. An extensive secretory apparatus and endomembrane system are presumably needed to synthesize and secrete the ECM, but structural details of such a system have not been fully characterized. Penium margaritaceum is a valuable unicellular model charophyte for studying secretion dynamics. We report that Penium has a highly organized endomembrane system, consisting of 150–200 non-mobile Golgi bodies that process and package ECM components into different sets of vesicles that traffic to the cortical cytoplasm, where they are transported around the cell by cytoplasmic streaming. At either fixed or transient areas, specific cytoplasmic vesicles fuse with the plasma membrane and secrete their constituents. Extracellular polysaccharide (EPS) production was observed to occur in one location of the Golgi body and sometimes in unique Golgi hybrids. Treatment of cells with brefeldin A caused disruption of the Golgi body, and inhibition of EPS secretion and cell wall expansion. The structure of the endomembrane system in Penium provides mechanistic insights into how extant charophytes generate large quantities of ECM, which in their ancestors facilitated the colonization of land.

Ultrastructure of the female reproductive organs (ovary, vitellaria, and Mehlis' gland) of Halipegus eccentricus (Trematoda: Derogenidae)

1986 ◽  
Vol 64 (10) ◽  
pp. 2203-2212 ◽  
Author(s):  
Jon M. Holy ◽  
Darwin D. Wittrock
Keyword(s):  
Cell Types ◽  
Reproductive Organs ◽  
Golgi Body ◽  
Digenetic Trematode ◽  
Secretory Cells ◽  
Cortical Granules ◽  
Golgi Bodies ◽  
Transmission Electron ◽  
Vitelline Cells ◽  
Female Reproductive Organs

The female reproductive organs (ovary, vitellaria, and Mehlis' gland) of the digenetic trematode Halipegus eccentricus were studied by transmission electron microscopy. Oocytes entered diplotene while in the ovary and produced cortical granules and lipid bodies. Vitelline cells produced large amounts of eggshell protein but no yolk bodies. Two types of Mehlis' gland secretory cells were present, distinguishable by the morphology of their rough endoplasmic reticulum, Golgi bodies, and secretory bodies, and by the persistence of recognizable secretory material within the ootype lumen after exocytosis. In an attempt to standardize the nomenclature regarding the cell types of the Mehlis' gland, a classification that takes into account these four criteria is proposed. Two basic types of Golgi body organization were noted for the cells of the female reproductive system: a stack of flattened cisternae (Mehlis' gland alpha cells) and spherical Golgi bodies with vesicular cisternae (oocytes, vitelline cells, and Mehlis' gland beta cells).

scholarly journals Lava Lamp, a Novel Peripheral Golgi Protein, Is Required for Drosophila melanogaster Cellularization

2000 ◽  
Vol 151 (4) ◽  
pp. 905-918 ◽  
Author(s):  
John C. Sisson ◽  
Christine Field ◽  
Richard Ventura ◽  
Anne Royou ◽  
William Sullivan
Keyword(s):  
Membrane Trafficking ◽  
Biochemical Analysis ◽  
Potent Inhibitor ◽  
Animal Cell ◽  
Coiled Coil ◽  
Brefeldin A ◽  
Microtubule Associated Proteins ◽  
Golgi Bodies ◽  
Associated Proteins ◽  
Golgi Protein

Drosophila cellularization and animal cell cytokinesis rely on the coordinated functions of the microfilament and microtubule cytoskeletal systems. To identify new proteins involved in cellularization and cytokinesis, we have conducted a biochemical screen for microfilament/microtubule-associated proteins (MMAPs). 17 MMAPs were identified; seven have been previously implicated in cellularization and/or cytokinesis, including KLP3A, Anillin, Septins, and Dynamin. We now show that a novel MMAP, Lava Lamp (Lva), is also required for cellularization. Lva is a coiled-coil protein and, unlike other proteins previously implicated in cellularization or cytokinesis, it is Golgi associated. Our functional analysis shows that cellularization is dramatically inhibited upon injecting anti–Lva antibodies (IgG and Fab) into embryos. In addition, we show that brefeldin A, a potent inhibitor of membrane trafficking, also inhibits cellularization. Biochemical analysis demonstrates that Lva physically interacts with the MMAPs Spectrin and CLIP190. We suggest that Lva and Spectrin may form a Golgi-based scaffold that mediates the interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization. Our results are consistent with the idea that animal cell cytokinesis depends on both actomyosin-based contraction and Golgi-derived membrane secretion.

The organization of tip-growth-related organelles and microtubules revealed by quantitative analysis of freeze-substituted oomycete hyphae

1989 ◽  
Vol 93 (1) ◽  
pp. 41-52
Author(s):  
I. BRENT HEATH ◽  
SUSAN G.W. KAMINSKYJ
Keyword(s):  
Golgi Body ◽  
Cell Periphery ◽  
Cross Sectional ◽  
Saprolegnia Ferax ◽  
Cytoskeleton Organization ◽  
Golgi Bodies ◽  
Section Electron ◽  
Serial Section Electron Microscopy ◽  
Body Production ◽  
Actin Cables

The distribution of organelles and microtubules in hyphal tips of the oomycete, Saprolegnia ferax, were quantitatively determined at high resolution from serial-section electron microscopy of freeze-substituted cells. All the organelles and the microtubules were non-uniformly distributed, each showing a characteristic longitudinal gradient starting at a different point behind the tip. In addition, when the cytoplasmic cross-sectional area was divided into radial regions, all organelles occurred preferentially in either the central (mitochondria and Golgi bodies) or the peripheral (microtubules, wall vesicles and spherical vesicles) region. The nuclei were so large as to span both regions but were always oriented with their centrioles facing the plasmalemma. Microtubules occurred in the extreme tips, became more abundant sub-apically, were predominantly short but increased in mean length with distance from the tip. The correlated patterns of organelle and cytoskeleton organization from this and previous work show that neither the microtubules nor the detected arrays of actin are sufficient to account for most organelle arrangements. However, on the basis of the distribution and orientation of the predominantly elongated wall vesicles, we suggest that the wall vesicles travel radially from their origin at the centrally located Golgi bodies to the cell periphery where they are transported longitudinally to the hyphal tip in conjunction with the plasmalemma-associated actin cables. Our data also suggest that the hyphae contain a cortical ectoplasm with which the nuclei interact, at least in part, via their centrioles and centriole-associated microtubules, and whose mechanical integrity is increased by both the peripheral actin cables and a high density of microtubules. We suggest that the endoplasm is less strong and has physiological properties that enhance the differentiation of endoplasmic reticulum and nuclear envelope into Golgi body production.

The Golgi Material and Mitochondria in the Salivary Glands of the Larva of Drosophila Melanogaster

1948 ◽  
Vol s3-89 (8) ◽  
pp. 401-414
Author(s):  
W. SIANG HSU
Keyword(s):  
Salivary Glands ◽  
Golgi Body ◽  
Anterior Portion ◽  
Golgi Bodies ◽  
Gland Cells ◽  
Salivary Gland Cells ◽  
Visible Part ◽  
Show Evidence ◽  
Storage Granules ◽  
Reserve Food

1. The salivary glands in the larvae of Drosophila show evidence of serving two functions: (1) production of digestive secretion, (2) accumulation of reserve food for the period of pupation. The two functions proceed simultaneously within the same cell during certain stages of its development. 2. A single droplet of digestive material has been seen to originate and grow within each Golgi body in the gland-cells. When a certain size is reached the droplet is released into the cytoplasm and by the fusion of two or more of them bigger vacuoles are formed. The secretory material is discharged into the lumen by means of a merocrine mechanism. Neither mitochondria nor nucleus has been observed to take any visible part in the elaboration of secretion droplets. 3. The storage granules found in older and larger cells have been observed to be direct transformations of chondriomites, and neither the Golgi material nor the nucleus shows any sign of participation in the formation of these granules. 4. From the standpoint of morphology and behaviour, the Golgi bodies found in the salivary gland cells are the same as found in the cells of the glandular portion of the proventriculus and the epithelium of the anterior portion of the midgut of the larva. 5. My observations do not lend themselves convincingly to a two-component conception of the structure of Golgi bodies.

scholarly journals Brefeldin A promotes the appearance of oligosaccharyl phosphates derived from Glc3Man9GlcNAc2-PP-dolichol within the endomembrane system of HepG2 cells

2016 ◽  
Vol 57 (8) ◽  
pp. 1477-1491 ◽  
Author(s):  
Ahmad Massarweh ◽  
Michaël Bosco ◽  
Soria Iatmanen-Harbi ◽  
Clarice Tessier ◽  
Laura Amana ◽  
...  
Keyword(s):  
Hepg2 Cells ◽  
Brefeldin A ◽  
Endomembrane System

Effects of brefeldin A on the endomembrane system and germ tube formation of the tetraspore of Gelidium floridanum (Rhodophyta, Florideophyceae)

2014 ◽  
Vol 50 (3) ◽  
pp. 577-586 ◽  
Author(s):  
Carmen Simioni ◽  
Ticiane Rover ◽  
Éder C. Schmidt ◽  
Marthiellen R. de L. Felix ◽  
Luz Karime Polo ◽  
...  
Keyword(s):  
Germ Tube ◽  
Brefeldin A ◽  
Tube Formation ◽  
Endomembrane System ◽  
Gelidium Floridanum

scholarly journals Draft genome of the aquatic moss Fontinalis antipyretica (Fontinalaceae, Bryophyta)

Gigabyte ◽  
2020 ◽  
Vol 2020 ◽  
pp. 1-9
Author(s):  
Jin Yu ◽  
Linzhou Li ◽  
Sibo Wang ◽  
Shanshan Dong ◽  
Ziqiang Chen ◽  
...  
Keyword(s):  
Vascular Plants ◽  
Aquatic Plant ◽  
De Novo ◽  
Draft Genome ◽  
Nuclear Genome ◽  
Sister Group ◽  
Plant Genome ◽  
Fontinalis Antipyretica ◽  
Aquatic Moss ◽  
Colonization Of Land

Mosses comprise one of three lineages forming a sister group to extant vascular plants. Having emerged from an early split in the diversification of embryophytes, mosses may offer complementary insights into the evolution of traits following the transition to, and colonization of, land. Here, we report the draft nuclear genome of Fontinalis antipyretica (Fontinalaceae, Hypnales), a charismatic aquatic moss that is widespread in temperate regions of the Northern Hemisphere. We sequenced and de novo-assembled its genome using the 10X Genomics method. The genome comprises 385.2 Mbp, with a scaffold N50 of 45.8 Kbp. The assembly captured 87.2% of the 430 genes in the BUSCO Viridiplantae odb10 dataset. The newly generated F. antipyretica genome is the third moss genome, and the second seedless aquatic plant genome, to be sequenced and assembled to date.

scholarly journals RemA (YlzA) and RemB (YaaB) Regulate Extracellular Matrix Operon Expression and Biofilm Formation in Bacillus subtilis

2009 ◽  
Vol 191 (12) ◽  
pp. 3981-3991 ◽  
Author(s):  
Jared T. Winkelman ◽  
Kris M. Blair ◽  
Daniel B. Kearns
Keyword(s):  
Extracellular Matrix ◽  
Bacillus Subtilis ◽  
Biofilm Formation ◽  
Extracellular Polysaccharide ◽  
Pellicle Formation ◽  
Multicellular Aggregates ◽  
The Matrix ◽  
Matrix Components ◽  
Operon Expression ◽  
Motility Inhibition

ABSTRACT Biofilms are multicellular aggregates stabilized by an extracellular matrix. In Bacillus subtilis, the biofilm matrix is composed of an extracellular polysaccharide and the secreted protein TasA. Expression of both of the matrix components is repressed by the DNA-binding master regulator, SinR. Here we identify two small protein regulators of the extracellular matrix: RemA (formerly YlzA) and RemB (formerly YaaB). Mutation of RemA or RemB impairs pellicle formation, complex colony architecture, and motility inhibition in a sinR mutant background. Both proteins are required for the activation of the matrix biosynthesis operons and appear to act in parallel to SinR and two other known biofilm regulators, AbrB and DegU.

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