scholarly journals Alterations in Detergent-Resistant Plasma Membrane Microdomains in Arabidopsis thaliana During Cold Acclimation

2008 ◽  
Vol 50 (2) ◽  
pp. 341-359 ◽  
Author(s):  
Anzu Minami ◽  
Masayuki Fujiwara ◽  
Akari Furuto ◽  
Yoichiro Fukao ◽  
Tetsuro Yamashita ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Plasma Membrane ◽  
Cold Acclimation ◽  
Membrane Microdomains ◽  
Plasma Membrane Microdomains

124. Alterations of plasma membrane microdomains in oat and rye during cold acclimation

Cryobiology ◽  
2010 ◽  
Vol 61 (3) ◽  
pp. 399-400
Author(s):  
Daisuke Takahashi ◽  
Akari Furuto ◽  
Anzu Minami ◽  
Matsuo Uemura
Keyword(s):  
Plasma Membrane ◽  
Cold Acclimation ◽  
Membrane Microdomains ◽  
Plasma Membrane Microdomains

scholarly journals Flotillin microdomains interact with the cortical cytoskeleton to control uropod formation and neutrophil recruitment

2010 ◽  
Vol 191 (4) ◽  
pp. 771-781 ◽  
Author(s):  
Alexander Ludwig ◽  
Grant P. Otto ◽  
Kirsi Riento ◽  
Emily Hams ◽  
Padraic G. Fallon ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Ex Vivo ◽  
Neutrophil Migration ◽  
Neutrophil Recruitment ◽  
Membrane Microdomains ◽  
Neutrophil Chemotaxis ◽  
Myosin Iia ◽  
Plasma Membrane Microdomains ◽  
Cortical Cytoskeleton

We studied the function of plasma membrane microdomains defined by the proteins flotillin 1 and flotillin 2 in uropod formation and neutrophil chemotaxis. Flotillins become concentrated in the uropod of neutrophils after exposure to chemoattractants such as N-formyl-Met-Leu-Phe (fMLP). Here, we show that mice lacking flotillin 1 do not have flotillin microdomains, and that recruitment of neutrophils toward fMLP in vivo is reduced in these mice. Ex vivo, migration of neutrophils through a resistive matrix is reduced in the absence of flotillin microdomains, but the machinery required for sensing chemoattractant functions normally. Flotillin microdomains specifically associate with myosin IIa, and spectrins. Both uropod formation and myosin IIa activity are compromised in flotillin 1 knockout neutrophils. We conclude that the association between flotillin microdomains and cortical cytoskeleton has important functions during neutrophil migration, in uropod formation, and in the regulation of myosin IIa.

scholarly journals Topography of plasma membrane microdomains and its consequences for mast cell signaling

2006 ◽  
Vol 36 (10) ◽  
pp. 2795-2806 ◽  
Author(s):  
Petr Heneberg ◽  
Pavel Lebduška ◽  
L'ubica Dráberová ◽  
Jan Korb ◽  
Petr Dráber
Keyword(s):  
Mast Cell ◽  
Plasma Membrane ◽  
Cell Signaling ◽  
Membrane Microdomains ◽  
Plasma Membrane Microdomains

scholarly journals Yeast cell wall integrity sensors form specific plasma membrane microdomains important for signalling

2016 ◽  
Vol 18 (9) ◽  
pp. 1251-1267 ◽  
Author(s):  
Christian Kock ◽  
Henning Arlt ◽  
Christian Ungermann ◽  
Jürgen J. Heinisch
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Yeast Cell ◽  
Cell Wall Integrity ◽  
Yeast Cell Wall ◽  
Membrane Microdomains ◽  
Plasma Membrane Microdomains

scholarly journals DC-SIGN and Influenza Hemagglutinin Dynamics in Plasma Membrane Microdomains Are Markedly Different

2011 ◽  
Vol 100 (11) ◽  
pp. 2662-2670 ◽  
Author(s):  
Michelle S. Itano ◽  
Aaron K. Neumann ◽  
Ping Liu ◽  
Feng Zhang ◽  
Enrico Gratton ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Microdomains ◽  
Influenza Hemagglutinin ◽  
Plasma Membrane Microdomains

scholarly journals Palmitoylated Cysteines in Chikungunya Virus nsP1 Are Critical for Targeting to Cholesterol-Rich Plasma Membrane Microdomains with Functional Consequences for Viral Genome Replication

2020 ◽  
Vol 94 (10) ◽  
Author(s):  
William Bakhache ◽  
Aymeric Neyret ◽  
Eric Bernard ◽  
Andres Merits ◽  
Laurence Briant
Keyword(s):  
Plasma Membrane ◽  
Lipid Bilayers ◽  
Functional Role ◽  
Membrane Microdomains ◽  
Genome Replication ◽  
Functional Importance ◽  
Late Endosomes ◽  
Plasma Membrane Microdomains ◽  
Insight Into

ABSTRACT In mammalian cells, alphavirus replication complexes are anchored to the plasma membrane. This interaction with lipid bilayers is mediated through the viral methyl/guanylyltransferase nsP1 and reinforced by palmitoylation of cysteine residue(s) in the C-terminal region of this protein. Lipid content of membranes supporting nsP1 anchoring remains poorly studied. Here, we explore the membrane binding capacity of nsP1 with regard to cholesterol. Using the medically important chikungunya virus (CHIKV) as a model, we report that nsP1 cosegregates with cholesterol-rich detergent-resistant membrane microdomains (DRMs), also called lipid rafts. In search for the critical factor for cholesterol partitioning, we identify nsP1 palmitoylated cysteines as major players in this process. In cells infected with CHIKV or transfected with CHIKV trans-replicase plasmids, nsP1, together with the other nonstructural proteins, are detected in DRMs. While the functional importance of CHIKV nsP1 preference for cholesterol-rich membrane domains remains to be determined, we observed that U18666A- and imipramine-induced sequestration of cholesterol in late endosomes redirected nsP1 to these compartments and simultaneously dramatically decreased CHIKV genome replication. A parallel study of Sindbis virus (SINV) revealed that nsP1 from this divergent alphavirus displays a low affinity for cholesterol and only moderately segregates with DRMs. Behaviors of CHIKV and SINV with regard to cholesterol, therefore, match with the previously reported differences in the requirement for nsP1 palmitoylation, which is dispensable for SINV but strictly required for CHIKV replication. Altogether, this study highlights the functional importance of nsP1 segregation with DRMs and provides new insight into the functional role of nsP1 palmitoylated cysteines during alphavirus replication. IMPORTANCE Functional alphavirus replication complexes are anchored to the host cell membranes through the interaction of nsP1 with the lipid bilayers. In this work, we investigate the importance of cholesterol for such an association. We show that nsP1 has affinity for cholesterol-rich membrane microdomains formed at the plasma membrane and identify conserved palmitoylated cysteine(s) in nsP1 as the key determinant for cholesterol affinity. We demonstrate that drug-induced cholesterol sequestration in late endosomes not only redirects nsP1 to this compartment but also dramatically decreases genome replication, suggesting the functional importance of nsP1 targeting to cholesterol-rich plasma membrane microdomains. Finally, we show evidence that nsP1 from chikungunya and Sindbis viruses displays different sensitivity to cholesterol sequestering agents that parallel with their difference in the requirement for nsP1 palmitoylation for replication. This research, therefore, gives new insight into the functional role of palmitoylated cysteines in nsP1 for the assembly of functional alphavirus replication complexes in their mammalian host.

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