On the existence of endocytosis driven by membrane phase separations

Hilgemann, Donald W.; Lin, Mei Jung; Fine, Michael; Deisl, Christine

doi:10.1016/j.bbamem.2019.06.006

Cited by 29 publications

(37 citation statements)

References 115 publications

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“…Endocytosis of the entrapped fluid phase and plasma membrane proteins comes next, the preferred cargo of the flotillin-demarked vesicles being GPI-anchored proteins due to their raft localization ( Figure 2). Fekri et al [34] have pointed out that the USBM-induced endocytosis shares similarities with "lipid driven" MEND described by Hilgemann and coworkers [114]. Indeed, MEND also requires tyrosine phosphorylation of proteins and zDHHC5/2-dependent palmitoylation of cell surface proteins.…”

Section: Flotillins Associate With Plasma Membrane Raftsmentioning

confidence: 76%

“…zDHHC5 also mediates S-palmitoylation of cell surface proteins required for so-called massive endocytosis (MEND) thought to originate from ordered regions of the plasma membrane (rafts?) [114]. An intriguing relation of MEND to endocytosis involving flotillins has been suggested [34] and is discussed below.…”

Section: Flotillin-mediated Endocytosis Requires Protein S-palmitoylamentioning

confidence: 96%

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Flotillins: At the Intersection of Protein S-Palmitoylation and Lipid-Mediated Signaling

Kwiatkowska

Matveichuk

Fronk

et al. 2020

IJMS

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Flotillin-1 and flotillin-2 are ubiquitously expressed, membrane-associated proteins involved in multifarious cellular events from cell signaling, endocytosis, and protein trafficking to gene expression. They also contribute to oncogenic signaling. Flotillins bind the cytosolic leaflet of the plasma membrane and endomembranes and, upon hetero-oligomerization, serve as scaffolds facilitating the assembly of multiprotein complexes at the membrane–cytosol interface. Additional functions unique to flotillin-1 have been discovered recently. The membrane-binding of flotillins is regulated by S-palmitoylation and N-myristoylation, hydrophobic interactions involving specific regions of the polypeptide chain and, to some extent, also by their oligomerization. All these factors endow flotillins with an ability to associate with the sphingolipid/cholesterol-rich plasma membrane domains called rafts. In this review, we focus on the critical input of lipids to the regulation of the flotillin association with rafts and thereby to their functioning. In particular, we discuss how the recent developments in the field of protein S-palmitoylation have contributed to the understanding of flotillin1/2-mediated processes, including endocytosis, and of those dependent exclusively on flotillin-1. We also emphasize that flotillins affect directly or indirectly the cellular levels of lipids involved in diverse signaling cascades, including sphingosine-1-phosphate and PI(4,5)P2. The mutual relations between flotillins and distinct lipids are key to the regulation of their involvement in numerous cellular processes.

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Section: Flotillins Associate With Plasma Membrane Raftsmentioning

confidence: 76%

Section: Flotillin-mediated Endocytosis Requires Protein S-palmitoylamentioning

confidence: 96%

Flotillins: At the Intersection of Protein S-Palmitoylation and Lipid-Mediated Signaling

Kwiatkowska

Matveichuk

Fronk

et al. 2020

IJMS

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“…The L o domains in the bilayer used in our study are designed to represent the sphingolipid-and cholesterol-rich lipid rafts present in the cytoplasmic membrane of eukaryotic cells, which are membrane domains that play important roles in membrane trafficking and signal transduction. 11,13 Thus, the localization of Qdots with the L o domains are likely to have important implications in the Qdot interactions, uptake, and impact in eukaryotic cells.…”

Section: Preferential Interaction Of Qdots With the L D /L O Phase Bomentioning

confidence: 99%

“…9 One route of NP uptake into eukaryotic cells is through lipid raft-mediated endocytosis. 10,11 Lipid rafts in eukaryotic cells are membrane nanodomains enriched in sphingolipids and cholesterol or other sterols, 12 which play an important role in both membrane trafficking and signal transduction. 11,13 To understand the complex interactions between NPs and cells, supported lipid bilayers (SLBs) are often used as a model for the plasma membrane.…”

Section: Introductionmentioning

confidence: 99%

“…10,11 Lipid rafts in eukaryotic cells are membrane nanodomains enriched in sphingolipids and cholesterol or other sterols, 12 which play an important role in both membrane trafficking and signal transduction. 11,13 To understand the complex interactions between NPs and cells, supported lipid bilayers (SLBs) are often used as a model for the plasma membrane. [14][15][16][17] While SLBs lack the chemical complexity of intact cells, they enable controlled and systematic study of the chemical components that serve important roles in the function of the cell membrane.…”

Section: Introductionmentioning

confidence: 99%

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Preferential interactions of primary amine-terminated quantum dots with membrane domain boundaries and lipid rafts revealed with nanometer resolution

Mensch

Melby

Laudadio

et al. 2020

Environ. Sci.: Nano

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The initial interactions of engineered nanoparticles (NPs) with living cells are governed by physicochemical properties of the NP and the molecular composition and structure of the cell membrane. Eukaryotic cell membranes contain lipid raftsliquid-ordered nanodomains involved in membrane trafficking and molecular signaling. However, the impact of these membrane structures on cellular interactions of NPs remains unclear.Here we investigate the role of membrane domains in the interactions of primary amine-terminated quantum dots (Qdots) with liquid-ordered domains or lipid rafts in model membranes and intact cells, respectively.Using correlative atomic force and fluorescence microscopy, we found that the Qdots preferentially localized to boundaries between liquid-ordered and liquid-disordered phases in supported bilayers. The Qdots also induced holes at these phase boundaries. Using super resolution fluorescence microscopy (STORM), we found that the Qdots preferentially co-localized with lipid rafts in the membrane of intact trout gill epithelial cellsa model cell type for environmental exposures. Our observations uncovered preferential interactions of amineterminated Qdots with liquid-ordered domains and their boundaries, possibly due to membrane curvature at phase boundaries creating energetically favorable sites for NP interactions. The preferential interaction of the Qdots with lipid rafts supports their potential internalization via lipid raft-mediated endocytosis and interactions with raft-resident signaling molecules.The initial interactions of engineered nanoparticles (NPs) at the cell membrane govern NP internalization and impact on cellular functions. These interactions depend on physicochemical properties of the NP and the molecular structure of the cell membrane. Liquid-ordered domains, or lipid rafts, are key structures in eukaryotic cell membranes but their role in NP interactions is unclear. We focus on quantum dots (Qdots)technologically relevant NPs with broad applications and concerns over their environmental release. We show that primary amine-terminated Qdots preferentially interact with liquidordered domain boundaries in bilayers and with lipid rafts in intact cells. These findings shed new light on mechanisms underlying NP-cell interactions and ultimately contribute to predictive evaluations of environmental health and safety for the use of NPs.

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Cholesterol-dependent endocytosis of GPCRs: implications in pathophysiology and therapeutics

Kumar

Chattopadhyay

2021

Biophys Rev

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On the existence of endocytosis driven by membrane phase separations

Cited by 29 publications

References 115 publications

Flotillins: At the Intersection of Protein S-Palmitoylation and Lipid-Mediated Signaling

Flotillins: At the Intersection of Protein S-Palmitoylation and Lipid-Mediated Signaling

Preferential interactions of primary amine-terminated quantum dots with membrane domain boundaries and lipid rafts revealed with nanometer resolution

Cholesterol-dependent endocytosis of GPCRs: implications in pathophysiology and therapeutics

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