Neuronal Plasma Membrane Dynamics Evoked by Osmomechanical Perturbations

1998 ◽  
Vol 166 (3) ◽  
pp. 223-235 ◽  
Author(s):  
L.R. Mills ◽  
C.E. Morris
Keyword(s):  
Plasma Membrane ◽  
Membrane Dynamics ◽  
Neuronal Plasma Membrane

scholarly journals Measurement of dynamic membrane mechanosensation using optical tweezers

2021 ◽  
Author(s):  
Xuanling Li ◽  
Xing Liu ◽  
Xiaoyu Song ◽  
Yinmei Li ◽  
Ming Li ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Optical Tweezers ◽  
Environmental Changes ◽  
Quantitative Measure ◽  
Relaxation Curve ◽  
Membrane Dynamics ◽  
Molecular Organization ◽  
Cytoskeletal Remodeling ◽  
Relaxation Curves ◽  
Membrane Tether

Abstract Many cellular processes are orchestrated by dynamic changes in the plasma membrane to form membrane projections and endocytic vesicles in response to extracellular environmental changes. Our previous studies show that ARF6-ACAP4-ezrin signaling regulates membrane dynamics and curvature in response to EGF stimulation. However, there is no quantitative measurement to relate molecular organization of membrane cytoskeletal remodeling to stimulus-elicited mechanosensation on the plasma membrane. Optical tweezers is a powerful tool in the study of membrane tension. Comparing to pulling out an entire membrane tether at one time, the step-like method is more efficient because multiple relaxation curves can be obtained from one membrane tether. Fewer models describe relaxation curves to characterize mechanical properties of cell membrane. Here we establish a new method to measure the membrane relaxation curve of HeLa cells judged by the relationship between membrane tether diameter and tensions. We obtained effective viscosities and static tensions by fitting relaxation curves to our model. We noticed the delicate structure of relaxation curves contains information of cytoskeletal remodeling and lateral protein diffusion. Our study established a quantitative measure to characterize the mechanosensation of epithelial cells in response to stimulus-elicited membrane dynamics.

scholarly journals Dynamics and organization of proteins in the neuronal plasma membrane

2020 ◽  
Vol 169 ◽  
pp. 108043 ◽  
Author(s):  
Antoine Triller ◽  
Marianne Renner ◽  
Daniel Choquet
Keyword(s):  
Plasma Membrane ◽  
Neuronal Plasma Membrane

scholarly journals Endocytosis: a review of mechanisms and plasma membrane dynamics

1983 ◽  
Vol 210 (1) ◽  
pp. 1-13 ◽  
Author(s):  
J M Besterman ◽  
R B Low
Keyword(s):  
Plasma Membrane ◽  
Membrane Dynamics

scholarly journals HIV-1 requires Arf6-mediated membrane dynamics to efficiently enter and infect T lymphocytes

2011 ◽  
Vol 22 (8) ◽  
pp. 1148-1166 ◽  
Author(s):  
Laura García-Expósito ◽  
Jonathan Barroso-González ◽  
Isabel Puigdomènech ◽  
José-David Machado ◽  
Julià Blanco ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
T Lymphocytes ◽  
Viral Entry ◽  
Membrane Trafficking ◽  
Membrane Dynamics ◽  
Viral Fusion ◽  
Viral Attachment ◽  
Immunodeficiency Virus ◽  
Vesicular Stomatitis ◽  
Hiv 1

As the initial barrier to viral entry, the plasma membrane along with the membrane trafficking machinery and cytoskeleton are of fundamental importance in the viral cycle. However, little is known about the contribution of plasma membrane dynamics during early human immunodeficiency virus type 1 (HIV-1) infection. Considering that ADP ribosylation factor 6 (Arf6) regulates cellular invasion via several microorganisms by coordinating membrane trafficking, our aim was to study the function of Arf6-mediated membrane dynamics on HIV-1 entry and infection of T lymphocytes. We observed that an alteration of the Arf6–guanosine 5′-diphosphate/guanosine 5′-triphosphate (GTP/GDP) cycle, by GDP-bound or GTP-bound inactive mutants or by specific Arf6 silencing, inhibited HIV-1 envelope–induced membrane fusion, entry, and infection of T lymphocytes and permissive cells, regardless of viral tropism. Furthermore, cell-to-cell HIV-1 transmission of primary human CD4+T lymphocytes was inhibited by Arf6 knockdown. Total internal reflection fluorescence microscopy showed that Arf6 mutants provoked the accumulation of phosphatidylinositol-(4,5)-biphosphate–associated structures on the plasma membrane of permissive cells, without affecting CD4-viral attachment but impeding CD4-dependent HIV-1 entry. Arf6 silencing or its mutants did not affect fusion, entry, and infection of vesicular stomatitis virus G–pseudotyped viruses or ligand-induced CXCR4 or CCR5 endocytosis, both clathrin-dependent processes. Therefore we propose that efficient early HIV-1 infection of CD4+T lymphocytes requires Arf6-coordinated plasma membrane dynamics that promote viral fusion and entry.

scholarly journals Dynamics of Glycine Receptor Insertion in the Neuronal Plasma Membrane

2001 ◽  
Vol 21 (14) ◽  
pp. 5036-5044 ◽  
Author(s):  
Madelaine Rosenberg ◽  
Jochen Meier ◽  
Antoine Triller ◽  
Christian Vannier
Keyword(s):  
Plasma Membrane ◽  
Glycine Receptor ◽  
Neuronal Plasma Membrane

scholarly journals Paralemmin, a Prenyl-Palmitoyl–anchored Phosphoprotein Abundant in Neurons and Implicated in Plasma Membrane Dynamics and Cell Process Formation

1998 ◽  
Vol 143 (3) ◽  
pp. 795-813 ◽  
Author(s):  
Christian Kutzleb ◽  
Gabriele Sanders ◽  
Raina Yamamoto ◽  
Xiaolu Wang ◽  
Beate Lichte ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Plasma Membranes ◽  
Species Conservation ◽  
Cell Types ◽  
Membrane Dynamics ◽  
Morphological Properties ◽  
Developmentally Regulated ◽  
Membrane Flow ◽  
Western Blots ◽  
Process Formation

We report the identification and initial characterization of paralemmin, a putative new morphoregulatory protein associated with the plasma membrane. Paralemmin is highly expressed in the brain but also less abundantly in many other tissues and cell types. cDNAs from chicken, human, and mouse predict acidic proteins of 42 kD that display a pattern of sequence cassettes with high inter-species conservation separated by poorly conserved linker sequences. Prenylation and palmitoylation of a COOH-terminal cluster of three cysteine residues confers hydrophobicity and membrane association to paralemmin. Paralemmin is also phosphorylated, and its mRNA is differentially spliced in a tissue-specific and developmentally regulated manner. Differential splicing, lipidation, and phosphorylation contribute to electrophoretic heterogeneity that results in an array of multiple bands on Western blots, most notably in brain. Paralemmin is associated with the cytoplasmic face of the plasma membranes of postsynaptic specializations, axonal and dendritic processes and perikarya, and also appears to be associated with an intracellular vesicle pool. It does not line the neuronal plasmalemma continuously but in clusters and patches. Its molecular and morphological properties are reminiscent of GAP-43, CAP-23, and MARCKS, proteins implicated in plasma membrane dynamics. Overexpression in several cell lines shows that paralemmin concentrates at sites of plasma membrane activity such as filopodia and microspikes, and induces cell expansion and process formation. The lipidation motif is essential for this morphogenic activity. We propose a function for paralemmin in the control of cell shape, e.g., through an involvement in membrane flow or in membrane–cytoskeleton interaction.

Chapter 7 Compartmentalizing the Neuronal Plasma Membrane

2008 ◽  
pp. 303-389 ◽  
Author(s):  
Zofia M. Lasiecka ◽  
Chan Choo Yap ◽  
Max Vakulenko ◽  
Bettina Winckler
Keyword(s):  
Plasma Membrane ◽  
Neuronal Plasma Membrane

Kir6.1 Is the Principal Pore-Forming Subunit of Astrocyte but Not Neuronal Plasma Membrane K-ATP Channels

2001 ◽  
Vol 18 (6) ◽  
pp. 671-690 ◽  
Author(s):  
Achim Thomzig ◽  
Mareike Wenzel ◽  
Christine Karschin ◽  
Misty J. Eaton ◽  
Serguei N. Skatchkov ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Neuronal Plasma Membrane

Insulin modulates neuronal plasma membrane development in human fetal spinal cord neurons in culture

1986 ◽  
Vol 65 (3) ◽  
pp. 283-286 ◽  
Author(s):  
L.M. Garcia-Segura ◽  
E.R. Barnea ◽  
W. Biggers ◽  
F. Naftolin ◽  
M.K. Sanyal
Keyword(s):  
Spinal Cord ◽  
Plasma Membrane ◽  
Spinal Cord Neurons ◽  
Neuronal Plasma Membrane ◽  
Membrane Development
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