scholarly journals S-acylation controls SARS-CoV-2 membrane lipid organization and enhances infectivity

Author(s):  
Francisco S. Mesquita ◽  
Laurence Abrami ◽  
Oksana Sergeeva ◽  
Priscilla Turelli ◽  
Enya Qing ◽  
...  
1986 ◽  
Vol 126 (3) ◽  
pp. 379-388 ◽  
Author(s):  
Brian J. Del Buono ◽  
Patrick L. Williamson ◽  
Robert A. Schlegel

2019 ◽  
Vol 116 (42) ◽  
pp. 21274-21284 ◽  
Author(s):  
Dingquan Huang ◽  
Yanbiao Sun ◽  
Zhiming Ma ◽  
Meiyu Ke ◽  
Yong Cui ◽  
...  

Plasmodesmata (PD) are plant-specific membrane-lined channels that create cytoplasmic and membrane continuities between adjacent cells, thereby facilitating cell–cell communication and virus movement. Plant cells have evolved diverse mechanisms to regulate PD plasticity in response to numerous environmental stimuli. In particular, during defense against plant pathogens, the defense hormone, salicylic acid (SA), plays a crucial role in the regulation of PD permeability in a callose-dependent manner. Here, we uncover a mechanism by which plants restrict the spreading of virus and PD cargoes using SA signaling by increasing lipid order and closure of PD. We showed that exogenous SA application triggered the compartmentalization of lipid raft nanodomains through a modulation of the lipid raft-regulatory protein, Remorin (REM). Genetic studies, superresolution imaging, and transmission electron microscopy observation together demonstrated that Arabidopsis REM1.2 and REM1.3 are crucial for plasma membrane nanodomain assembly to control PD aperture and functionality. In addition, we also found that a 14-3-3 epsilon protein modulates REM clustering and membrane nanodomain compartmentalization through its direct interaction with REM proteins. This study unveils a molecular mechanism by which the key plant defense hormone, SA, triggers membrane lipid nanodomain reorganization, thereby regulating PD closure to impede virus spreading.


2021 ◽  
Vol 131 (8) ◽  
Author(s):  
Patrick J. Ferrara ◽  
Xin Rong ◽  
J. Alan Maschek ◽  
Anthony R.P. Verkerke ◽  
Piyarat Siripoksup ◽  
...  

1989 ◽  
Vol 138 (1) ◽  
pp. 61-69 ◽  
Author(s):  
Brian J. Del Buono ◽  
Scott M. White ◽  
Patrick L. Williamson ◽  
Robert A. Schlegel

1988 ◽  
Vol 44 (5) ◽  
pp. 337-344 ◽  
Author(s):  
Leslie McEvoy ◽  
Robert A. Schlegel ◽  
Patrick Williamson ◽  
Brian J. Del Buono

1983 ◽  
Vol 18 ◽  
pp. 1-6 ◽  
Author(s):  
E.K. Michaelis ◽  
H.H. Chang ◽  
S. Roy ◽  
J.A. McFaul ◽  
J.D. Zimbrick

2019 ◽  
Author(s):  
Patrick J. Ferrara ◽  
Xin Rong ◽  
J. Alan Maschek ◽  
Anthony R.P. Verkerke ◽  
Piyarat Siripoksup ◽  
...  

AbstractAberrant lipid metabolism promotes the development of skeletal muscle insulin resistance, but the exact identity of lipid-mediated mechanisms relevant to human obesity remains unclear. A comprehensive lipidomic analyses of primary myocytes from lean insulin-sensitive (LN) and obese insulin-resistant (OB) individuals revealed several species of lysophospholipids (lyso-PL) that were differentially-abundant. These changes coincided with greater expression of lysophosphatidylcholine acyltransferase 3 (LPCAT3), an enzyme involved in phospholipid transacylation (Lands cycle). Strikingly, mice with skeletal muscle-specific knockout of LPCAT3 (LPCAT3-MKO) exhibited greater muscle lyso-PC/PC, concomitant with greater insulin sensitivity in vivo and insulin-stimulated skeletal muscle glucose uptake ex vivo. Absence of LPCAT3 reduced phospholipid packing of the cellular membranes and increased plasma membrane lipid clustering, suggesting that LPCAT3 affects insulin receptor phosphorylation by modulating plasma membrane lipid organization. In conclusion, obesity accelerates the skeletal muscle Lands cycle, whose consequence might induce the disruption of plasma membrane organization that suppresses muscle insulin action.


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