scholarly journals Ankyrin G Organizes Membrane Components to Promote Coupling of Cell Mechanics and Metabolism

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Kris DeMali ◽  
Alica Salvi ◽  
Jennifer Bays ◽  
Samantha Mackin
Author(s):  
Alicia M. Salvi ◽  
Jennifer L. Bays ◽  
Samantha R. Mackin ◽  
René-Marc Mege ◽  
Kris A. DeMali

2016 ◽  
Author(s):  
Christophe Leterrier ◽  
Nadine Clerc ◽  
Fanny Rueda-Boroni ◽  
Audrey Montersino ◽  
Bénédicte Dargent ◽  
...  

The axon initial segment (AIS) is a specialized neuronal compartment that plays a key role in neuronal development and excitability. It concentrates multiple ion channels and cell adhesion molecules. The anchoring of these AIS membrane components is known to be highly dependent of the scaffold protein ankyrin G (ankG) but whether ankG membrane partners play a reciprocal role in ankG targeting and stabilization has not been studied yet. In cultured hippocampal neurons and cortical organotypic slices, we found that shRNA-mediated knockdown of ankG membrane partners led to a decrease of ankG concentration and perturbed the AIS formation and maintenance. These perturbations were rescued by expressing an AIS-targeted sodium channel, or a minimal construct containing the ankyrin-binding domain of Nav1.2 and a membrane anchor. We thus demonstrate that a tight and precocious association of ankG to its membrane partners is crucial for the establishment and maintenance of the AIS.


Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.


Author(s):  
Michael Edidin

Cell surface membranes are based on a fluid lipid bilayer and models of the membranes' organization have emphasised the possibilities for lateral motion of membrane lipids and proteins within the bilayer. Two recent trends in cell and membrane biology make us consider ways in which membrane organization works against its inherent fluidity, localizing both lipids and proteins into discrete domains. There is evidence for such domains, even in cells without obvious morphological polarity and organization [Table 1]. Cells that are morphologically polarised, for example epithelial cells, raise the issue of membrane domains in an accute form.The technique of fluorescence photobleaching and recovery, FPR, was developed to measure lateral diffusion of membrane components. It has also proven to be a powerful tool for the analysis of constraints to lateral mobility. FPR resolves several sorts of membrane domains, all on the micrometer scale, in several different cell types.


2019 ◽  
Vol 20 (3) ◽  
pp. 255-262 ◽  
Author(s):  
Sounik Manna ◽  
Munmun Ghosh ◽  
Ranadhir Chakraborty ◽  
Sudipto Ghosh ◽  
Santi M. Mandal

Succumbing to Multi-Drug Resistant (MDR) bacteria is a great distress to the recent health care system. Out of the several attempts that have been made to kill MDR pathogens, a few gained short-lived success. The failures, of the discovered or innovated antimicrobials, were mostly due to their high level of toxicity to hosts and the phenomenal rate of developing resistance by the pathogens against the new arsenal. Recently, a few quantum dots were tested against the pathogenic bacteria and therefore, justified for potential stockpiling of next-generation antibacterial agents. The key players for antimicrobial properties of quantum dots are considered to be Reactive Oxygen Species (ROS). The mechanism of reaction between bacteria and quantum dots needs to be better understood. They are generally targeted towards the cell wall and membrane components as lipoteichoic acid and phosphatidyl glycerol of bacteria have been documented here. In this paper, we have attempted to simulate ZnS quantum dots and have analysed their mechanism of reaction as well as binding potential to the above bacterial membrane components using CDOCKER. Results have shown a high level of antibacterial activity towards several pathogenic bacteria which specify their potentiality for future generation antibacterial drug development.


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