Golgi apparatus activity and membrane flow during scale biogenesis in the green flagellateScherffelia dubia (Prasinophyceae). I: Flagellar regeneration

PROTOPLASMA ◽  
1986 ◽  
Vol 130 (2-3) ◽  
pp. 186-198 ◽  
Author(s):  
G. I. McFadden ◽  
M. Melkonian
Planta ◽  
2000 ◽  
Vol 210 (4) ◽  
pp. 551-562 ◽  
Author(s):  
Lara Perasso ◽  
Andrea Grunow ◽  
Ines Maria Brüntrup ◽  
Barbara Bölinger ◽  
Michael Melkonian ◽  
...  

Author(s):  
D. James Morré ◽  
E. L. Vigil ◽  
T. W. Keenan

Concepts of membrane flow and membrane differentiation are combined to explain the formation of eukaryotic endomembranes along a sequence of cell components in subcellular developmental pathways. Membrane differentiation is the gradual conversion of membranes from one type to another and is documented by comparisons of enzymatic activities, lipid composition and progressive modification of the proteins and lipids of membranes along the endoplasmic reticulum (ER)-Golgi apparatus (GA)-secretory vesicle-plasma membrane (PM) export route. The biochemical studies show the transitional nature of GA membranes first revealed by morphological studies. Membrane dimensions and staining characteristics change progressively from ER-like to PM-like across the stacked cisternae from the forming to the maturing face of the apparatus. Membrane flow is the physical transfer of membrane from one cell component to another.


1984 ◽  
Vol 72 (1) ◽  
pp. 89-100
Author(s):  
H.J. Sluiman

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.


1985 ◽  
Vol 101 (3) ◽  
pp. 725-734 ◽  
Author(s):  
D B Williams ◽  
S J Swiedler ◽  
G W Hart

The intracellular transport of two closely related membrane glycoproteins was studied in the murine B cell lymphoma line, AKTB-1b. Using pulse-chase radiolabeling, the kinetics of appearance of the class I histocompatibility antigens, H-2Kk and H-2Dk, at the cell surface were compared and found to be remarkably different. Newly synthesized H-2Kk is transported rapidly such that all radiolabeled molecules reach the surface within 1 h. In contrast, the H-2Dk antigen is transported slowly with a half-time of 4-5 h. The rates of surface appearance for the two antigens closely resemble the rates at which their Asn-linked oligosaccharides mature from endoglucosaminidase H (endo H)-sensitive to endo H-resistant forms, a process that occurs in the Golgi apparatus. This suggests that the rate-limiting step in the transport of H-2Dk to the cell surface occurs before the formation of endo H-resistant oligosaccharides in the Golgi apparatus. Subcellular fractionation experiments confirmed this conclusion by identifying the endoplasmic reticulum (ER) as the site where the H-2Dk antigen accumulates. The retention of this glycoprotein in the ER does not appear to be due to a lack of solubility or an inability of the H-2Dk heavy chain to associate with beta 2-microglobulin. Our data is inconsistent with a passive membrane flow mechanism for the intracellular transport of membrane glycoproteins. Rather, it suggests that one or more receptors localized to the ER membrane may mediate the selective transport of membrane glycoproteins out of the ER to the Golgi apparatus. The fact that H-2Kk and H-2Dk are highly homologous (greater than or equal to 80%) indicates that this process can be strongly influenced by limited alterations in protein structure.


Author(s):  
Béatrice Satiat-Jeunemaitre ◽  
Jancy Henderson ◽  
David Evans ◽  
Kim Crooks ◽  
Mark Fricker ◽  
...  

In plant cells, as in animal cells, many macromolecules and membranes are transported by vesicle vectors through both the exocytotic and endocytotic pathways. In order to elucidate the mechanisms and molecular events of such trafficking we are using a set of drugs known to perturb membrane flow in plant cells in combination with immunocytochemical studies using a bank of monoclonal antibodies to various components of the endomembrane system and cell surface. In animal cells, one such drug, Brefeldin A, a fungal fatty acid derivative which causes disruption of the Golgi apparatus, has recently been used as a tool to dissect the mechanisms of vesicle flow from the endoplasmic reticulum to the Golgi apparatus and down the cisternae of the Golgi stack (1). It has been demonstrated that BFA also has a dramatic effect on the Golgi apparatus in higher plant cells (2,3,4).In this paper we report on recent work on the disruption of the plant Golgi apparatus with BFA and the redistribution of endomembrane marker epitopes after drug treatment of roots and suspension culture cells.


1998 ◽  
Vol 142 (1) ◽  
pp. 25-38 ◽  
Author(s):  
Jan Willem Kok ◽  
Teresa Babia ◽  
Catalin M. Filipeanu ◽  
Adriaan Nelemans ◽  
Gustavo Egea ◽  
...  

In this study, we show that an inhibitor of sphingolipid biosynthesis, d,l-threo-1-phenyl-2- decanoylamino-3-morpholino-1-propanol (PDMP), inhibits brefeldin A (BFA)-induced retrograde membrane transport from Golgi to endoplasmic reticulum (ER). If BFA treatment was combined with or preceded by PDMP administration to cells, disappearance of discrete Golgi structures did not occur. However, when BFA was allowed to exert its effect before PDMP addition, PDMP could not “rescue” the Golgi compartment. Evidence is presented showing that this action of PDMP is indirect, which means that the direct target is not sphingolipid metabolism at the Golgi apparatus. A fluorescent analogue of PDMP, 6-(N-[7-nitro-2,1,3-benzoxadiazol-4-yl]amino)hexanoyl-PDMP (C6-NBD-PDMP), did not localize in the Golgi apparatus. Moreover, the effect of PDMP on membrane flow did not correlate with impaired C6-NBD-sphingomyelin biosynthesis and was not mimicked by exogenous C6-ceramide addition or counteracted by exogenous C6-glucosylceramide addition. On the other hand, the PDMP effect was mimicked by the multidrug resistance protein inhibitor MK571. The effect of PDMP on membrane transport correlated with modulation of calcium homeostasis, which occurred in a similar concentration range. PDMP released calcium from at least two independent calcium stores and blocked calcium influx induced by either extracellular ATP or thapsigargin. Thus, the biological effects of PDMP revealed a relation between three important physiological processes of multidrug resistance, calcium homeostasis, and membrane flow in the ER/ Golgi system.


1983 ◽  
Vol 96 (5) ◽  
pp. 1197-1207 ◽  
Author(s):  
C Tougard ◽  
D Louvard ◽  
R Picart ◽  
A Tixier-Vidal

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.


1971 ◽  
Vol 26 (10) ◽  
pp. 1031-1039 ◽  
Author(s):  
Werner W. Franke ◽  
D. James Morre ◽  
Barbara Deumling ◽  
Ronald D. Cheetham ◽  
Jürgen Kartenbeck ◽  
...  

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.


Biomembranes ◽  
1971 ◽  
pp. 95-104 ◽  
Author(s):  
D. James Morré ◽  
W. W. Franke ◽  
B. Deumling ◽  
S. E. Nyquist ◽  
L. Ovtracht

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