A pathway of plasma membrane biogenesis bypassing the Golgi apparatus during cell division in the green alga Cylindrocapsa geminella

1984 ◽  
Vol 72 (1) ◽  
pp. 89-100
Author(s):  
H.J. Sluiman
Keyword(s):  
Plasma Membrane ◽  
Cell Division ◽  
Golgi Apparatus ◽  
Cell Plate ◽  
Membrane Biogenesis ◽  
Membrane Flow ◽  
Septum Formation ◽  
Primary Septum ◽  
Rough Er ◽  
And Function

Cell division in Cylindrocapsa geminella, in particular the mode of septum membrane biogenesis, has been studied with the transmission electron microscope. Septum formation takes place in a narrow layer of cytoplasm separating post-mitotic nuclei. First, each daughter nucleus develops a wide cytoplasmic pocket (invagination) containing numerous strands of rough endoplasmic reticulum (ER). Next, a proliferation of rough ER is observed in the equatorial zone of cytoplasm, which invariably contains a small number of widely scattered microtubules. The equatorially aligned cisternae of rough ER produce smooth-membraned vesicles, interpreted as smooth ER, which subsequently coalesce to form the membranous transverse septum. Thus, primary septum formation does not follow any of the two previously known basic cytokinetic patterns in green plants (i.e. plasma membrane furrowing and cell-plate formation), but instead represents a novel type of membrane flow, which effectively bypasses the Golgi apparatus. This pathway of membrane flow has remained largely ignored in current concepts of endomembrane structure and function in eukaryotes. However, it appears to be more widespread than has previously been recognized, especially in autospore-producing green algae and in red algae during the formation of tetraspores. It may represent an evolutionary intermediate type of cell division between the supposedly primitive method of plasma membrane furrowing and the more advanced cell-plate system.

Microfilaments and cytoplasmic microtubules in cell division cycle mutants of Schizosaccharomyces pombe

1980 ◽  
Vol 26 (2) ◽  
pp. 250-254 ◽  
Author(s):  
E. Streiblová ◽  
M. Girbardt
Keyword(s):  
Plasma Membrane ◽  
Cell Division ◽  
Schizosaccharomyces Pombe ◽  
Cell Division Cycle ◽  
Restrictive Temperature ◽  
Septum Formation ◽  
Cytoplasmic Microtubules

The occurrence of axial cytoplasmic microtubules (25 nm in diameter) and of microfilaments (7 nm in diameter) associated in bundles just below the plasma membrane of the yeast Schizosaccharomyces pombe is described. Both types of cytoplasmic filamentous structures were present in the cell division cycle mutant cdc 12–112 of this fungus incubated for 6 h at the restrictive temperature of 35 °C. Microtubules and microfilaments probably function in septum formation and (or) in the volume-related control of the terminal phenotype of the mutant.

Mesosome-like Structures in a Blue-green Alga, Phormidium Luridum

1970 ◽  
Vol 28 ◽  
pp. 180-181
Author(s):  
Mercedes R. Edwards
Keyword(s):  
Plasma Membrane ◽  
Cell Division ◽  
Dna Replication ◽  
Green Alga ◽  
Photosynthetic Bacteria ◽  
Blue Green Alga ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Lamellar Structures ◽  
Septum Formation

The invagination of the plasma membrane (plasmalemma) to form vesicular or lamellar structures, usually called mesosomes (l) or plasmalemmosomes (2), has been extensively documented in bacteria (3) and more recently also in lower eucaryotes (e.g., the fungi, 4). Such structures have “been implicated in septum formation (i.e., cell division of gram-positive bacteria), in respiratory reactions, and in DNA replication.In photosynthetic bacteria, such as Rhodospirilium rubrum, vesicular structures derived from the plasma membrane were shown by Drews and Giesbrecht (5) to give rise to thylakoids (photosynthetic vesicles or chromatophores). Continuation between the plasma and thylakoidal membranes is readily seen in R. rubrum (6).

scholarly journals The rough endoplasmic reticulum and the Golgi apparatus visualized using specific antibodies in normal and tumoral prolactin cells in culture.

1983 ◽  
Vol 96 (5) ◽  
pp. 1197-1207 ◽  
Author(s):  
C Tougard ◽  
D Louvard ◽  
R Picart ◽  
A Tixier-Vidal
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Primary Cultures ◽  
Gh3 Cells ◽  
Membrane Flow ◽  
Golgi Membranes ◽  
Membrane Components ◽  
Golgi Zone

Antibodies directed against membrane components of dog pancreas rough endoplasmic reticulum (A-RER) and rat liver Golgi apparatus (A-Golgi) (Louvard, D., H. Reggio, and G. Warren, 1982, J. Cell Biol. 92:92-107) have been applied to cultured rat prolactin (PRL) cells, either normal cells in primary cultures, or clonal GH3 cells. In normal PRL cells, the A-RER stained the membranes of the perinuclear cisternae as well as those of many parallel RER cisternae. The A-Golgi stained part of the Golgi membranes. In the stacks it stained the medial saccules and, with a decreasing intensity, the saccules of the trans side, as well as, in some cells, a linear cisterna in the center of the Golgi zone. It also stained the membrane of many small vesicles as well as that of lysosomelike structures in all cells. In contrast, it never stained the secretory granule membrane, except at the level of very few segregating granules on the trans face of the Golgi zone. In GH3 cells the A-RER stained the membrane of the perinuclear cisternae, as well as that of short discontinuous flat cisternae. The A-Golgi stained the same components of the Golgi zone as in normal PRL cells. In some cells of both types the A-Golgi also stained discontinuous patches on the plasma membrane and small vesicles fusing with the plasma membrane. Immunostaining of Golgi membranes revealed modifications of membrane flow in relation to either acute stimulation of PRL release by thyroliberin or inhibition of basal secretion by monensin.

Synthesis and Turnover of Membrane Proteins in Rat Liver: An Examination of the Membrane Flow Hypothesis

1971 ◽  
Vol 26 (10) ◽  
pp. 1031-1039 ◽  
Author(s):  
Werner W. Franke ◽  
D. James Morre ◽  
Barbara Deumling ◽  
Ronald D. Cheetham ◽  
Jürgen Kartenbeck ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Golgi Apparatus ◽  
Plasma Membranes ◽  
Degradation Kinetics ◽  
Specific Radioactivity ◽  
Membrane Flow ◽  
Rapid Turnover ◽  
Associated Proteins

The kinetics of synthesis and degradation of the protein constituents of nuclear membranes, endoplasmic reticulum membranes (rough-surfaced microsomes), Golgi apparatus membranes and plasma membranes were determined following a single administration of L- [guanido-14C] arginine by intraperitoneal injection. Membrane protein was determined as the fraction which resists sonication and sequential extrations with 1.5 M KCl, 0.1% deoxycholate and water to remove intravesicular, intracisternal (secretory), nucleo-, adsorbed and ribosome-associated proteins.The order of maximum labeling of membrane proteins was a) endoplasmic reticulum (nuclear membrane), b) Golgi apparatus, and c) plasma membrane. Rapid decreases in specific radioactivity followed maximal labeling of endoplasmic reticulum and Golgi apparatus membranes. These rapid turnover components of endoplasmic reticulum and Golgi apparatus were sufficient to account for labeling of plasma membranes via a flow mechanism.Incorporation of radioactivity into plasma membranes showed two distinct phases. The ultrastructural features underlying the biphasic pattern of incorporation into plasma membranes are discussed.Following initial incorporation and rapid turnover, membrane proteins were characterized by degradation kinetics approximating 1st order. Rates of degradation for Golgi apparatus and plasma membranes were faster than those for nuclear envelope and endoplasmic reticulum membranes.Assuming steady state conditions, an absolute synthetic rate of 7.1 mpg/min/avergage hepatocyte was calculated for membrane proteins of the plasma membrane.The results are compatible with intracellular movement and conversion of rough endoplasmic reticulum to plasma membrane via the membranes of the Golgi apparatus, i. e., membrane flow. Additionally, the kinetics indicate that membrane synthesis and transfer is restricted to specific parts of the endoplasmic reticulum and Golgi apparatus.

Golgi Apparatus Function in Membrane Flow and Differentiation: Origin of Plasma Membrane from Endoplasmic Reticulum

Biomembranes ◽  
1971 ◽  
pp. 95-104 ◽  
Author(s):  
D. James Morré ◽  
W. W. Franke ◽  
B. Deumling ◽  
S. E. Nyquist ◽  
L. Ovtracht
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Membrane Flow ◽  
Apparatus Function

scholarly journals Extracellular cell wall β(1,3)glucan is required to couple septation to actomyosin ring contraction

2013 ◽  
Vol 203 (2) ◽  
pp. 265-282 ◽  
Author(s):  
Javier Muñoz ◽  
Juan Carlos G. Cortés ◽  
Matthias Sipiczki ◽  
Mariona Ramos ◽  
José Angel Clemente-Ramos ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Animal Cells ◽  
Contractile Ring ◽  
Septum Formation ◽  
Main Cell ◽  
Primary Septum ◽  
Pulling Forces

Cytokinesis has been extensively studied in different models, but the role of the extracellular cell wall is less understood. Here we studied this process in fission yeast. The essential protein Bgs4 synthesizes the main cell wall β(1,3)glucan. We show that Bgs4-derived β(1,3)glucan is required for correct and stable actomyosin ring positioning in the cell middle, before the start of septum formation and anchorage to the cell wall. Consequently, β(1,3)glucan loss generated ring sliding, oblique positioned rings and septa, misdirected septum synthesis indicative of relaxed rings, and uncoupling between a fast ring and membrane ingression and slow septum synthesis, suggesting that cytokinesis can progress with defective septum pushing and/or ring pulling forces. Moreover, Bgs4-derived β(1,3)glucan is essential for secondary septum formation and correct primary septum completion. Therefore, our results show that extracellular β(1,3)glucan is required for cytokinesis to connect the cell wall with the plasma membrane and for contractile ring function, as proposed for the equivalent extracellular matrix in animal cells.

Confocal microscopy of the cytoskeleton in living plant cells following microinjection of fluorescent probes

1993 ◽  
Vol 51 ◽  
pp. 130-131
Author(s):  
Ann Cleary
Keyword(s):  
Cell Division ◽  
Fluorescent Probes ◽  
Actin Filaments ◽  
Intracellular Transport ◽  
Cell Structure ◽  
Plant Cells ◽  
Cell Plate ◽  
Cell Cortex ◽  
Living Plant ◽  
Rhodamine Phalloidin

Microinjection of fluorescent probes into living plant cells reveals new aspects of cell structure and function. Microtubules and actin filaments are dynamic components of the cytoskeleton and are involved in cell growth, division and intracellular transport. To date, cytoskeletal probes used in microinjection studies have included rhodamine-phalloidin for labelling actin filaments and fluorescently labelled animal tubulin for incorporation into microtubules. From a recent study of Tradescantia stamen hair cells it appears that actin may have a role in defining the plane of cell division. Unlike microtubules, actin is present in the cell cortex and delimits the division site throughout mitosis. Herein, I shall describe actin, its arrangement and putative role in cell plate placement, in another material, living cells of Tradescantia leaf epidermis.The epidermis is peeled from the abaxial surface of young leaves usually without disruption to cytoplasmic streaming or cell division. The peel is stuck to the base of a well slide using 0.1% polyethylenimine and bathed in a solution of 1% mannitol +/− 1 mM probenecid.

scholarly journals Correlative AFM and fluorescence imaging demonstrate nanoscale membrane remodeling and ring-like and tubular structure formation by septins

Nanoscale ◽  
2021 ◽  
Author(s):  
Anthony Vial ◽  
Cyntia Taveneau ◽  
Luca Costa ◽  
brieuc chauvin ◽  
hussein nasrallah ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Division ◽  
Structure Formation ◽  
Fluorescence Imaging ◽  
Tubular Structure ◽  
Membrane Remodeling

Septins are ubiquitous cytoskeletal filaments that interact with the inner plasma membrane and are essential for cell division in eukaryotes. In cellular contexts, septins are often localized at micrometric gaussian...

scholarly journals Actin-membrane interaction in fibroblasts: what proteins are involved in this association?

1984 ◽  
Vol 99 (1) ◽  
pp. 95s-103s ◽  
Author(s):  
P Mangeat ◽  
K Burridge
Keyword(s):  
Plasma Membrane ◽  
Actin Filaments ◽  
Stress Fiber ◽  
Membrane Interaction ◽  
Microfilament Bundles ◽  
The Family ◽  
Form Part ◽  
Membrane Attachment ◽  
A Chain ◽  
And Function

In this review we discuss some of the proteins for which a role in linking actin to the fibroblast plasma membrane has been suggested. We focus on the family of proteins related to erythrocyte spectrin, proteins that have generally been viewed as having an organization and a function in actin-membrane attachment similar to those of erythrocyte spectrin. Experiments in which we precipitated the nonerythrocyte spectrin within living fibroblasts have led us to question this supposed similarity of organization and function of the nonerythrocyte and erythrocyte spectrins. Intracellular precipitation of fibroblast spectrin does not affect the integrity of the major actin-containing structures, the stress fiber microfilament bundles. Unexpectedly, however, we found that the precipitation of spectrin results in a condensation and altered distribution of the vimentin class of intermediate filaments in most cells examined. Although fibroblast spectrin may have a role in the attachment of some of the cortical, submembranous actin, it is surprising how little the intracellular immunoprecipitation of the spectrin affects the cells. Several proteins have been found concentrated at the ends of stress fibers, where the actin filaments terminate at focal contacts. Two of these proteins, alpha-actinin and fimbrin, have properties that suggest that they are not involved in the attachment of the ends of the bundles to the membrane but are more probably involved in the organization and cross-linking of the filaments within the bundles. On the other hand, vinculin and talin are two proteins that interact with each other and may form part of a chain of attachments between the ends of the microfilament bundles and the focal contact membrane. Their role in this attachment, however, has not been established and further work is needed to examine their interaction with actin and to identify any other components with which they may interact, particularly in the plasma membrane.

scholarly journals Mutations in GDAP1 Influence Structure and Function of the Trans-Golgi Network

2021 ◽  
Vol 22 (2) ◽  
pp. 914
Author(s):  
Katarzyna Binięda ◽  
Weronika Rzepnikowska ◽  
Damian Kolakowski ◽  
Joanna Kaminska ◽  
Andrzej Antoni Szczepankiewicz ◽  
...  
Keyword(s):  
Golgi Apparatus ◽  
Experimental Therapy ◽  
Negative Effects ◽  
Gene Encoding ◽  
Charcot Marie Tooth Disease ◽  
Terra Incognita ◽  
And Function ◽  
Golgi Network ◽  
Cell Phenotypes ◽  
Tooth Disease

Charcot-Marie-Tooth disease (CMT) is a heritable neurodegenerative disease that displays great genetic heterogeneity. The genes and mutations that underlie this heterogeneity have been extensively characterized by molecular genetics. However, the molecular pathogenesis of the vast majority of CMT subtypes remains terra incognita. Any attempts to perform experimental therapy for CMT disease are limited by a lack of understanding of the pathogenesis at a molecular level. In this study, we aim to identify the molecular pathways that are disturbed by mutations in the gene encoding GDAP1 using both yeast and human cell, based models of CMT-GDAP1 disease. We found that some mutations in GDAP1 led to a reduced expression of the GDAP1 protein and resulted in a selective disruption of the Golgi apparatus. These structural alterations are accompanied by functional disturbances within the Golgi. We screened over 1500 drugs that are available on the market using our yeast-based CMT-GDAP1 model. Drugs were identified that had both positive and negative effects on cell phenotypes. To the best of our knowledge, this study is the first report of the Golgi apparatus playing a role in the pathology of CMT disorders. The drugs we identified, using our yeast-based CMT-GDAP1 model, may be further used in translational research.

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