scholarly journals Shuttling of cellular proteins between the plasma membrane and nucleus (Review)

2021 ◽  
Vol 25 (1) ◽  
Author(s):  
Hua-Chuan Zheng ◽  
Hua-Mao Jiang
Keyword(s):  
Plasma Membrane ◽  
Cellular Proteins

PI(4,5)P2 Clustering and Its Impact on Biological Functions

2021 ◽  
Vol 90 (1) ◽  
Author(s):  
Yi Wen ◽  
Volker M. Vogt ◽  
Gerald W. Feigenson
Keyword(s):  
Plasma Membrane ◽  
Cell Biology ◽  
Cellular Proteins ◽  
Annual Review ◽  
Publication Date ◽  
Biological Functions ◽  
Cellular Functions ◽  
Dynamic Distribution ◽  
Multivalent Cation ◽  
Lipid Environment

Located at the inner leaflet of the plasma membrane, phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] comprises only 1–2 mol% of total PM lipids. With its synthesis and turnover both spatially and temporally regulated, PI(4,5)P2 recruits and interacts with hundreds of cellular proteins to support a broad spectrum of cellular functions. Several factors contribute to the versatile and dynamic distribution of PI(4,5)P2 in membranes. Physiological multivalent cations such as Ca2+ and Mg2+ can bridge between PI(4,5)P2 headgroups, forming nanoscopic PI(4,5)P2–cation clusters. The distinct lipid environment surrounding PI(4,5)P2 affects the degree of PI(4,5)P2 clustering. In addition, diverse cellular proteins interacting with PI(4,5)P2 can further regulate PI(4,5)P2 lateral distribution and accessibility. This review summarizes the current understanding of PI(4,5)P2 behavior in both cells and model membranes, with emphasis on both multivalent cation– and protein-induced PI(4,5)P2 clustering. Understanding the nature of spatially separated pools of PI(4,5)P2 is fundamental to cell biology. Expected final online publication date for the Annual Review of Biochemistry, Volume 90 is June 2021. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

scholarly journals Role of Plasma Membrane Lipid Microdomains in Respiratory Syncytial Virus Filament Formation

2003 ◽  
Vol 77 (3) ◽  
pp. 1747-1756 ◽  
Author(s):  
Lewis H. McCurdy ◽  
Barney S. Graham
Keyword(s):  
Plasma Membrane ◽  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Syncytium Formation ◽  
Membrane Lipid ◽  
Small Gtpase ◽  
Cellular Proteins ◽  
Lipid Microdomains ◽  
Protein F ◽  
Syncytial Virus

ABSTRACT The fusion protein (F) of respiratory syncytial virus (RSV) is the envelope glycoprotein responsible for the characteristic cytopathology of syncytium formation. RSV has been shown to bud from selective areas of the plasma membrane as pleomorphic virions, including both filamentous and round particles. With immunofluorescent microscopy, we demonstrated evidence of RSV filaments incorporating the fusion protein F and colocalizing with a lipid microdomain-specific fluorescent dye, 1,1-dihexadecyl-3,3,3,3-tetramethylindocarbocyanine perchlorate. Western blot analysis of Triton X-100 cold-extracted membrane fractions confirmed the presence of RSV proteins within the lipid microdomains. RSV proteins also colocalized with cellular proteins associated with lipid microdomains, caveolin-1, and CD44, as well as with RhoA, a small GTPase. ADP-ribosylation of RhoA by Clostridium botulinum exotoxin inactivated RhoA signaling and resulted in the absence of RSV-induced syncytia despite no significant change in viral titer. We demonstrated an overall decrease in both the number and length of the viral filaments and a shift in the localization of F to nonlipid microdomain regions of the membrane in the presence of C3 toxin. This suggests that the selective incorporation of RSV proteins into lipid microdomains during virus assembly may lead to critical interactions of F with cellular proteins, resulting in microvillus projections necessary for the formation of filamentous virus particles and syncytium formation. Thus, manipulation of membrane lipid microdomains may lead to alterations in the production of viral filaments and RSV pathogenesis and provide a new pharmacologic target for RSV therapy.

scholarly journals Hydrolase secretion is a consequence of membrane recycling.

1984 ◽  
Vol 98 (1) ◽  
pp. 246-252 ◽  
Author(s):  
T C Hohman ◽  
B Bowers
Keyword(s):  
Plasma Membrane ◽  
Culture Medium ◽  
The Other ◽  
Cellular Proteins ◽  
Cellular Activity ◽  
Lysosomal Hydrolases ◽  
Ph Shift ◽  
Ph Dependent ◽  
Secondary Lysosomes ◽  
Energy Dependent

Acanthamoeba releases lysosomal hydrolases continuously into the culture medium. This release is specific for lysosomal hydrolases, but not other cellular proteins, and is energy dependent. The secreted hydrolases can be separated into two groups on the basis of their secretion kinetics: one is secreted at approximately 15% of the cellular activity per hour and the other at approximately 5%. Intracellularly the lysosomal hydrolases are restricted almost exclusively to secondary lysosomes where the hydrolases demonstrate a differential pH-dependent binding to membrane. Hydrolase secretion is not the result of secondary lysosomes' fusing with the plasma membrane since soluble and particulate lysosomal contents are not released at the same rate. Together the data suggest that the secreted hydrolases are trapped in shuttle vesicles that cycle membrane from secondary lysosomes to the cell surface. The inner membrane and content of these vesicles undergo a marked pH shift when, following fragmentation from lysosomes, these vesicles fuse with plasma membrane. This rapid pH shift and the differential pH-dependent membrane binding of hydrolases appear to account for the heterogeneous hydrolase secretion kinetics.

scholarly journals Multiple Cellular Proteins Modulate the Dynamics of K-ras Association with the Plasma Membrane

2010 ◽  
Vol 99 (10) ◽  
pp. 3327-3335 ◽  
Author(s):  
Pinkesh Bhagatji ◽  
Rania Leventis ◽  
Rebecca Rich ◽  
Chen-ju Lin ◽  
John R. Silvius
Keyword(s):  
Plasma Membrane ◽  
Cellular Proteins

Heterogeneity of Size and Distribution of Intramembrane Particles in the Plasma Membrane of Yeast

1977 ◽  
Vol 35 ◽  
pp. 596-597
Author(s):  
E. Keyhani
Keyword(s):  
Plasma Membrane ◽  
Candida Utilis ◽  
Synthetic Medium ◽  
Freeze Fracture ◽  
Translational Diffusion ◽  
Yeast Cells ◽  
Distilled Water ◽  
Intramembrane Particles ◽  
The Matrix ◽  
Water Cell

The matrix of biological membranes consists of a lipid bilayer into which proteins or protein aggregates are intercalated. Freeze-fracture techni- ques permit these proteins, perhaps in association with lipids, to be visualized in the hydrophobic regions of the membrane. Thus, numerous intramembrane particles (IMP) have been found on the fracture faces of membranes from a wide variety of cells (1-3). A recognized property of IMP is their tendency to form aggregates in response to changes in experi- mental conditions (4,5), perhaps as a result of translational diffusion through the viscous plane of the membrane. The purpose of this communica- tion is to describe the distribution and size of IMP in the plasma membrane of yeast (Candida utilis).Yeast cells (ATCC 8205) were grown in synthetic medium (6), and then harvested after 16 hours of culture, and washed twice in distilled water. Cell pellets were suspended in growth medium supplemented with 30% glycerol and incubated for 30 minutes at 0°C, centrifuged, and prepared for freeze-fracture, as described earlier (2,3).

Organization of the Pellicle and the Muciferous Glands in Euglena Gracilis

1970 ◽  
Vol 28 ◽  
pp. 104-105
Author(s):  
Hilton H. Mollenhauer ◽  
W. Evans
Keyword(s):  
Plasma Membrane ◽  
Euglena Gracilis ◽  
Complex Forms ◽  
Secondary Periodicity

The pellicular structure of Euglena gracilis consists of a series of relatively rigid strips (Fig. 1) composed of ridges and grooves which are helically oriented along the cell and which fuse together into a common junction at either end of the cell. The strips are predominantly protein and consist in part of a series of fibers about 50 Å in diameter spaced about 85 Å apart and with a secondary periodicity of about 450 Å. Microtubules are also present below each strip (Fig. 1) and are often considered as part of the pellicular complex. In addition, there may be another fibrous component near the base of the pellicle which has not yet been very well defined.The pellicular complex lies underneath the plasma membrane and entirely within the cell (Fig. 1). Each strip of the complex forms an overlapping junction with the adjacent strip along one side of each groove (Fig. 1), in such a way that a certain amount of sideways movement is possible between one strip and the next.

Localization of Sodium in Normal and Inhibited Transporting Epithelia

1971 ◽  
Vol 29 ◽  
pp. 392-393
Author(s):  
G. I. Kaye ◽  
J. D. Cole
Keyword(s):  
Plasma Membrane ◽  
Similar Pattern ◽  
Fixation Method ◽  
Colonic Epithelium ◽  
Gallbladder Epithelium ◽  
Rabbit Colon ◽  
Rabbit Gallbladder

For a number of years we have used an adaptation of Komnick's KSb(OH)6-OsO4 fixation method for the localization of sodium in tissues in order to study transporting epithelia under a number of different conditions. We have shown that in actively transporting rabbit gallbladder epithelium, large quantities of NaSb(OH)6 precipitate are found in the distended intercellular compartment, while localization of precipitate is confined to the inner side of the lateral plasma membrane in inactive gallbladder epithelium. A similar pattern of distribution of precipitate has been demonstrated in human and rabbit colon in active and inactive states and in the inactive colonic epithelium of hibernating frogs.

Electron microscopy of endocardial cell populations

1978 ◽  
Vol 36 (2) ◽  
pp. 486-487
Author(s):  
T. G. Sarphie ◽  
C. R. Comer ◽  
D. J. Allen
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Cellular Transformation ◽  
Cell Populations ◽  
Cell Surfaces ◽  
Kb Cells ◽  
Dna Viruses ◽  
Cell Cycles ◽  
Ultrastructural Studies ◽  
Endocardial Cell

Previous ultrastructural studies have characterized surface morphology during norma cell cycles in an attempt to associate specific changes with specific metabolic processes occurring within the cell. It is now known that during the synthetic ("S") stage of the cycle, when DNA and other nuclear components are synthesized, a cel undergoes a doubling in volume that is accompanied by an increase in surface area whereby its plasma membrane is elaborated into a variety of processes originally referred to as microvilli. In addition, changes in the normal distribution of glycoproteins and polysaccharides derived from cell surfaces have been reported as depreciating after cellular transformation by RNA or DNA viruses and have been associated with the state of growth, irregardless of the rate of proliferation. More specifically, examination of the surface carbohydrate content of synchronous KB cells were shown to be markedly reduced as the cell population approached division Comparison of hamster kidney fibroblasts inhibited by vinblastin sulfate while in metaphase with those not in metaphase demonstrated an appreciable decrease in surface carbohydrate in the former.

Microanatomy of the Periplasm of Bacillus Licheniformis

1971 ◽  
Vol 29 ◽  
pp. 262-263
Author(s):  
B.K. Ghosh
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Bacillus Licheniformis ◽  
External Environment ◽  
Permeability Barrier ◽  
Periplasmic Space ◽  
Modified Technique ◽  
Gram Positive ◽  
Gram Negative ◽  
Gram Positive Bacteria

Periplasm of bacteria is the space outside the permeability barrier of plasma membrane but enclosed by the cell wall. The contents of this special milieu exterior could be regulated by the plasma membrane from the internal, and by the cell wall from the external environment of the cell. Unlike the gram-negative organism, the presence of this space in gram-positive bacteria is still controversial because it cannot be clearly demonstrated. We have shown the importance of some periplasmic bodies in the secretion of penicillinase from Bacillus licheniformis.In negatively stained specimens prepared by a modified technique (Figs. 1 and 2), periplasmic space (PS) contained two kinds of structures: (i) fibrils (F, 100 Å) running perpendicular to the cell wall from the protoplast and (ii) an array of vesicles of various sizes (V), which seem to have evaginated from the protoplast.

Changes Occur in Plasma Membrane Turnover when K562 Leukemia Cells are Induced to Differentiate

1982 ◽  
Vol 40 ◽  
pp. 286-287
Author(s):  
L. M. Marshall
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Intracellular Transport ◽  
Parent Cell ◽  
Membrane Turnover ◽  
Coated Pits ◽  
Surface Distribution ◽  
Specific Proteins ◽  
Erythroleukemic Cell ◽  
Specific Membrane

A human erythroleukemic cell line, metabolically blocked in a late stage of erythropoiesis, becomes capable of differentiation along the normal pathway when grown in the presence of hemin. This process is characterized by hemoglobin synthesis followed by rearrangement of the plasma membrane proteins and culminates in asymmetrical cytokinesis in the absence of nuclear division. A reticulocyte-like cell buds from the nucleus-containing parent cell after erythrocyte specific membrane proteins have been sequestered into its membrane. In this process the parent cell faces two obstacles. First, to organize its erythrocyte specific proteins at one pole of the cell for inclusion in the reticulocyte; second, to reduce or abolish membrane protein turnover since hemoglobin is virtually the only protein being synthesized at this stage. A means of achieving redistribution and cessation of turnover could involve movement of membrane proteins by a directional lipid flow. Generation of a lipid flow towards one pole and accumulation of erythrocyte-specific membrane proteins could be achieved by clathrin coated pits which are implicated in membrane endocytosis, intracellular transport and turnover. In non-differentiating cells, membrane proteins are turned over and are random in surface distribution. If, however, the erythrocyte specific proteins in differentiating cells were excluded from endocytosing coated pits, not only would their turnover cease, but they would also tend to drift towards and collect at the site of endocytosis. This hypothesis requires that different protein species are endocytosed by the coated vesicles in non-differentiating than by differentiating cells.

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