Pathogens: raft hijackers

Mañes, Santos; Real, Gustavo del; Martı́nez-A, Carlos

doi:10.1038/nri1129

Cited by 448 publications

(392 citation statements)

References 114 publications

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“…In the case of Alzheimer's amyloid b-protein, gangliosides in lipid microdomains ('lipid rafts') mediated the protein's aggregation [13]. Lipid rafts are composed of sphingomyelin, gangliosides, and cholesterol [14] and considered to be a platform of a large number of events in plasma membranes, including signal transductions and viral assembly and budding [15][16][17]. The formation of amyloid fibrils by hIAPP is also possibly mediated by gangliosides in lipid rafts on live cell membranes.…”

Section: Introductionmentioning

confidence: 99%

Ganglioside‐induced amyloid formation by human islet amyloid polypeptide in lipid rafts

Wakabayashi¹,

Matsuzaki²

2009

FEBS Letters

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Edited by Jesus Avila Keywords:Human islet amyloid polypeptide Amyloid fibril Ganglioside Cholesterol Lipid raft a b s t r a c t Human islet amyloid polypeptide (hIAPP) is the primary component of the amyloid deposits found in the pancreatic islets of patients with type 2 diabetes mellitus. However, it is unknown how amyloid fibrils are formed in vivo. In this study, we demonstrate that gangliosides play an essential role in the formation of amyloid deposits by hIAPP on plasma membranes. Amyloid fibrils accumulated in ganglioside-and cholesterol-rich microscopic domains ('lipid rafts'). The depletion of gangliosides or cholesterol significantly reduced the amount of amyloid deposited. These results clearly showed that the formation of amyloid fibrils was mediated by gangliosides in lipid rafts.

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Section: Introductionmentioning

confidence: 99%

Ganglioside‐induced amyloid formation by human islet amyloid polypeptide in lipid rafts

Wakabayashi¹,

Matsuzaki²

2009

FEBS Letters

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“…These domains are docking sites for many signaling molecules, and are origins for coordinated signaling 27-29 . Many microbial pathogens, including viruses, use lipid rafts for entry, trafficking, and budding 30,31 . In the present study, we set out to determine if integrin coordinates with EGFR to facilitate HCMV infection and if lipid rafts are involved in this coordination.…”

mentioning

confidence: 99%

Integrin αvβ3 is a coreceptor for human cytomegalovirus

Wang

Huang

Huong

et al. 2005

Nat Med

251

289

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HCMV is a widespread opportunistic pathogen that causes birth defects in newborns and severe disease in immunocompromised individuals. The broad tropism of HCMV infection suggests that it utilizes multiple receptors. We recently demonstrated that EGFR serves as a receptor for HCMV. Here we show that HCMV also uses integrin αvβ3 as a coreceptor. Upon infection, HCMV glycoproteins gB and gH independently bind to EGFR and αvβ3, respectively, to initiate viral entry and signaling. αvβ3 then translocates to lipid rafts where it interacts with EGFR to induce coordinated signaling. The coordination between EGFR and αvβ3 is essential for the early events of HCMV infection, including viral entry, RhoA downregulation, stress fiber disassembly, and viral nuclear trafficking. Our findings support a model where EGFR and αvβ3 work together as coreceptors for HCMV entry and signaling. This discovery is fundamental to understanding HCMV pathogenesis and developing treatment strategies targeted to viral receptors.Human cytomegalovirus (HCMV) is a β-group herpesvirus that causes severe complications in immunocompromised individuals. HCMV is also a leading cause of virus-associated birth defects, is associated with atherosclerosis and coronary restenosis, and has been implicated as a cofactor in the progression of HIV-1 infection 1-4 . The oncogenic potential of HCMV has also been demonstrated 5-7 .

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“…Lipid rafts are hypothesized to function by a process of compartmentalization (Simons and Ikonen 1997;Pierce 2002;Manes et al 2003;Pike 2003;Parton and Hancock 2004). In this model, interactions of molecules within the same raft are enhanced, while interactions of nonraft and raft molecules are inhibited due to their spatial segregation.…”

Section: Molecular Mechanisms Underlying Raft Formation and Functionmentioning

confidence: 99%

Lipid rafts, cholesterol, and the brain

2008

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SummaryLipid rafts are specialized membrane microdomains that serve as organizing centers for assembly of signaling molecules, influence membrane fluidity and trafficking of membrane proteins, and regulate different cellular processes such as neurotransmission and receptor trafficking. In this article, we provide an overview of current methods for studying lipid rafts and models for how lipid rafts might form and function. Next, we propose a potential mechanism for regulating lipid rafts in the brain via local control of cholesterol biosynthesis by neurotrophins and their receptors. Finally, we discuss evidence that altered cholesterol metabolism and/or lipid rafts play a critical role in the pathophysiology of multiple CNS disorders, including Smith-Lemli-Opitz syndrome, Huntington, Alzheimer's, and Niemman-Pick Type C diseases.

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Pathogens: raft hijackers

Cited by 448 publications

References 114 publications

Ganglioside‐induced amyloid formation by human islet amyloid polypeptide in lipid rafts

Ganglioside‐induced amyloid formation by human islet amyloid polypeptide in lipid rafts

Integrin αvβ3 is a coreceptor for human cytomegalovirus

Lipid rafts, cholesterol, and the brain

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