Lateral Membrane Heterogeneity Probed by FRET Spectroscopy and Microscopy

2012 ◽  
pp. 71-113 ◽  
Author(s):  
Luís M. S. Loura ◽  
Manuel Prieto
Keyword(s):  
Membrane Heterogeneity ◽  
Lateral Membrane

Membrane nanodomains: contribution of curvature and interaction with proteins and cytoskeleton

2015 ◽  
Vol 57 ◽  
pp. 109-119 ◽  
Author(s):  
Senthil Arumugam ◽  
Patricia Bassereau
Keyword(s):  
Phase Separation ◽  
Lipid Membranes ◽  
Effective Means ◽  
Membrane Domains ◽  
Significant Development ◽  
Membrane Heterogeneity ◽  
Lateral Membrane ◽  
Biological Functionality ◽  
Major Factors ◽  
Organizing Principles

The understanding of lipid membranes and their organization has undergone significant development with better techniques and therefore more resolved experiments. Many new factors and organizing principles have been discovered, and interplay between these factors is expected to result in rich functional behaviours. The major factors regulating the lateral membrane heterogeneity, apart from the well-studied phase separation, are cytoskeleton pinning, clustering of lipids and curvature. These factors are effective means to create membrane domains that provide rich biological functionality. We review the recent advances and concepts of membrane heterogeneity organization by curvature, cytoskeleton and clustering proteins.

scholarly journals Lateral Membrane Heterogeneity Regulates Viral-Induced Membrane Fusion during HIV Entry

2018 ◽  
Vol 19 (5) ◽  
pp. 1483 ◽  
Author(s):  
Rodion Molotkovsky ◽  
Veronika Alexandrova ◽  
Timur Galimzyanov ◽  
Irene Jiménez-Munguía ◽  
Konstantin Pavlov ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Induced Membrane ◽  
Membrane Heterogeneity ◽  
Lateral Membrane ◽  
Hiv Entry

What do nanometer molecular trajectories tell us about heterogeneous cell surface domaines?

1995 ◽  
Vol 53 ◽  
pp. 786-787
Author(s):  
Watt W. Webb
Keyword(s):  
Cell Surface ◽  
Lipid Membranes ◽  
Surface Proteins ◽  
Protein Diffusion ◽  
Coated Pits ◽  
Cell Surface Proteins ◽  
Membrane Heterogeneity ◽  
Fluorescence Photobleaching Recovery ◽  
Photobleaching Recovery ◽  
Plasma Membrane Heterogeneity

Plasma membrane heterogeneity is implicit in the existence of specialized cell surface organelles which are necessary for cellular function; coated pits, post and pre-synaptic terminals, microvillae, caveolae, tight junctions, focal contacts and endothelial polarization are examples. The persistence of these discrete molecular aggregates depends on localized restraint of the constituent molecules within specific domaines in the cell surface by strong intermolecular bonds and/or anchorage to extended cytoskeleton. The observed plasticity of many of organelles and the dynamical modulation of domaines induced by cellular signaling evidence evanescent intermolecular interactions even in conspicuous aggregates. There is also strong evidence that universal restraints on the mobility of cell surface proteins persist virtually everywhere in cell surfaces, not only in the discrete organelles. Diffusion of cell surface proteins is slowed by several orders of magnitude relative to corresponding protein diffusion coefficients in isolated lipid membranes as has been determined by various ensemble average methods of measurement such as fluorescence photobleaching recovery(FPR).

scholarly journals Interaction of phosphorylated Rab11-FIP2 with Eps15 regulates apical junction composition

2017 ◽  
Vol 28 (8) ◽  
pp. 1088-1100 ◽  
Author(s):  
Lynne A. Lapierre ◽  
Elizabeth H. Manning ◽  
Kenya M. Mitchell ◽  
Cathy M. Caldwell ◽  
James R. Goldenring
Keyword(s):  
Mdck Cells ◽  
Three Dimensional ◽  
3D Culture ◽  
Cyst Formation ◽  
Epithelial Polarity ◽  
Lateral Membrane ◽  
Low Calcium ◽  
Single Lumen ◽  
Apical Junctions ◽  
Temporal Localization

MARK2 regulates the establishment of polarity in Madin–Darby canine kidney (MDCK) cells in part through phosphorylation of serine 227 of Rab11-FIP2. We identified Eps15 as an interacting partner of phospho-S227-Rab11-FIP2 (pS227-FIP2). During recovery from low calcium, Eps15 localized to the lateral membrane before pS227-FIP2 arrival. Later in recovery, Eps15 and pS227-FIP2 colocalized at the lateral membrane. In MDCK cells expressing the pseudophosphorylated FIP2 mutant FIP2(S227E), during recovery from low calcium, Eps15 was trapped and never localized to the lateral membrane. Mutation of any of the three NPF domains within GFP-FIP2(S227E) rescued Eps15 localization at the lateral membrane and reestablished single-lumen cyst formation in GFP-FIP2(S227E)–expressing cells in three-dimensional (3D) culture. Whereas expression of GFP-FIP2(S227E) induced the loss of E-cadherin and occludin, mutation of any of the NPF domains of GFP-FIP2(S227E) reestablished both proteins at the apical junctions. Knockdown of Eps15 altered the spatial and temporal localization of pS227-FIP2 and also elicited formation of multiple lumens in MDCK 3D cysts. Thus an interaction of Eps15 and pS227-FIP2 at the appropriate time and location in polarizing cells is necessary for proper establishment of epithelial polarity.

scholarly journals DAAM1 stabilizes epithelial junctions by restraining WAVE complex–dependent lateral membrane motility

2016 ◽  
Vol 215 (4) ◽  
pp. 559-573 ◽  
Author(s):  
Tamako Nishimura ◽  
Shoko Ito ◽  
Hiroko Saito ◽  
Sylvain Hiver ◽  
Kenta Shigetomi ◽  
...  
Keyword(s):  
Actin Filaments ◽  
Junctional Complex ◽  
Lateral Membrane ◽  
Apical Junctional Complex ◽  
Cell Layers ◽  
Epithelial Junctions ◽  
Membrane Contacts ◽  
Epithelial Layers ◽  
Actin Cables ◽  
Wave Complex

Epithelial junctions comprise two subdomains, the apical junctional complex (AJC) and the adjacent lateral membrane contacts (LCs), that span the majority of the junction. The AJC is lined with circumferential actin cables, whereas the LCs are associated with less-organized actin filaments whose roles are elusive. We found that DAAM1, a formin family actin regulator, accumulated at the LCs, and its depletion caused dispersion of actin filaments at these sites while hardly affecting circumferential actin cables. DAAM1 loss enhanced the motility of LC-forming membranes, leading to their invasion of neighboring cell layers, as well as disruption of polarized epithelial layers. We found that components of the WAVE complex and its downstream targets were required for the elevation of LC motility caused by DAAM1 loss. These findings suggest that the LC membranes are motile by nature because of the WAVE complex, but DAAM1-mediated actin regulation normally restrains this motility, thereby stabilizing epithelial architecture, and that DAAM1 loss evokes invasive abilities of epithelial cells.

scholarly journals Remodeling the cell surface distribution of membrane proteins during the development of epithelial cell polarity.

1992 ◽  
Vol 116 (4) ◽  
pp. 889-899 ◽  
Author(s):  
D A Wollner ◽  
K A Krzeminski ◽  
W J Nelson
Keyword(s):  
Epithelial Cell ◽  
Membrane Proteins ◽  
Cell Surface ◽  
Mdck Cells ◽  
Apical Cell ◽  
Cell Contact ◽  
Surface Polarity ◽  
Lateral Membrane ◽  
E Cadherin ◽  
Cell Cell

The development of polarized epithelial cells from unpolarized precursor cells follows induction of cell-cell contacts and requires resorting of proteins into different membrane domains. We show that in MDCK cells the distributions of two membrane proteins, Dg-1 and E-cadherin, become restricted to the basal-lateral membrane domain within 8 h of cell-cell contact. During this time, however, 60-80% of newly synthesized Dg-1 and E-cadherin is delivered directly to the forming apical membrane and then rapidly removed, while the remainder is delivered to the basal-lateral membrane and has a longer residence time. Direct delivery of greater than 95% of these proteins from the Golgi complex to the basal-lateral membrane occurs greater than 48 h later. In contrast, we show that two apical proteins are efficiently delivered and restricted to the apical cell surface within 2 h after cell-cell contact. These results provide insight into mechanisms involved in the development of epithelial cell surface polarity, and the establishment of protein sorting pathways in polarized cells.

Correlation of Apical and Lateral Membrane Modulations of Maturation Ameloblasts

1985 ◽  
Vol 64 (8) ◽  
pp. 1055-1061 ◽  
Author(s):  
Z. Skobe ◽  
F. LaFrazia ◽  
K. Prostak
Keyword(s):  
Apical Membrane ◽  
Apical Cell ◽  
Matrix Proteins ◽  
Maturation Stage ◽  
Enamel Matrix ◽  
Enamel Matrix Proteins ◽  
Rat Incisor ◽  
Lateral Membrane ◽  
Apical Junctions ◽  
Scanning Electron

Maturation ameloblasts of rat incisor teeth have smooth-ended and ruffle-ended apical membrane configurations. It has also been reported that maturation ameloblasts have several lateral membrane configurations. The purpose of this study was to determine the correlation between the modulations of lateral and apical cell membranes of murine incisor ameloblasts in the maturation stage of amelogenesis. Maxillary and mandibular incisors were dissected, demineralized, embedded in paraffin, sectioned and then de-paraffinized, and the enamel organs were prepared for scanning electron microscopy. Additional mouse and rat incisor enamel organs were fixed and teased apart during dehydration, then observed in the SEM. The lengths of smooth- and ruffle-ended ameloblast segments were measured, and the site, length, and frequency of each lateral membrane configuration were determined within each segment. The lateral membrane configuration with folds forming from 12 to 14 channels around the periphery of the cells was most predominant in both smooth- and ruffle-ended cells. Cells surrounded by from six to eight channels were the only other lateral membrane configuration observed in ruffle-ended ameloblasts. Smooth-ended ameloblasts had lateral membrane configurations with either dense or sparse microvillous projections in addition to both types of channel cells. The observation that channelled extracellular spaces are always associated with ruffle-ended cells suggests that channels somehow function in conjunction with the ruffled apical membrane in resorption and removal of enamel matrix proteins. The smooth-ended ameloblasts lack tight apical junctions, and their microvillous lateral membranes permit the passage of plasma fluids around cells to the maturing enamel surface. Analysis of our data indicates that specific lateral membrane configurations are related to the type of apical membrane present.

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