A novel sphingomyelin/cholesterol domain‐specific probe reveals the dynamics of the membrane domains during virus release and in Niemann‐Pick type C

Makino, Asami; Abe, Mitsuhiro; Ishitsuka, Reiko; Murate, Motohide; Kishimoto, Tadamitsu; Sakaï, Shota; Hullin-Matsuda, Françoise; Shimada, Yukiko; Inaba, Takehiko; Miyatake, Hideyuki; Tanaka, Hideko; Kurahashi, Atsushi; Pack, Chan‐Gi; Kasai, Rinshi S.; Kubo, Shuku; Schieber, Nicole L.; Dohmae, Naoshi; Tochio, N.; Hagiwara, Kyoji; Sasaki, Yutaka; Aida, Yoko; Fujimori, Fumihiro; Kigawa, T.; Nishibori, Kozo; Parton, Robert G.; Kusumi, Akihiro; Sako, Yasushi; Anderluh, Gregor; Yamashita, Makoto; Kobayashi, Tetsuyuki; Greimel, Peter; Kobayashi, Toshihide

doi:10.1096/fj.201500075r

Cited by 38 publications

(49 citation statements)

References 106 publications

(152 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2014 ; Yalpani et al. 2017 ) and in the fungal sphingomyelin-binding/toxic proteins nakanori ( Makino et al. 2017 ) and pleurotolysin ( Lukoyanova et al.…”

Section: Resultsmentioning

confidence: 99%

Piercing Fishes: Porin Expansion and Adaptation to Hematophagy in the Vampire Snail Cumia reticulata

Gerdol

Cervelli

Oliverio

et al. 2018

Molecular Biology and Evolution

View full text Add to dashboard Cite

Cytolytic pore-forming proteins are widespread in living organisms, being mostly involved in both sides of the host–pathogen interaction, either contributing to the innate defense or promoting infection. In venomous organisms, such as spiders, insects, scorpions, and sea anemones, pore-forming proteins are often secreted as key components of the venom. Coluporins are pore-forming proteins recently discovered in the Mediterranean hematophagous snail Cumia reticulata (Colubrariidae), highly expressed in the salivary glands that discharge their secretion at close contact with the host. To understand their putative functional role, we investigated coluporins’ molecular diversity and evolutionary patterns. Coluporins is a well-diversified family including at least 30 proteins, with an overall low sequence similarity but sharing a remarkably conserved actinoporin-like predicted structure. Tracking the evolutionary history of the molluscan porin genes revealed a scattered distribution of this family, which is present in some other lineages of predatory gastropods, including venomous conoidean snails. Comparative transcriptomic analyses highlighted the expansion of porin genes as a lineage-specific feature of colubrariids. Coluporins seem to have evolved from a single ancestral porin gene present in the latest common ancestor of all Caenogastropoda, undergoing massive expansion and diversification in this colubrariid lineage through repeated gene duplication events paired with widespread episodic positive selection. As for other parasites, these findings are congruent with a “one-sided arms race,” equipping the parasite with multiple variants in order to broaden its host spectrum. Overall, our results pinpoint a crucial adaptive role for coluporins in the evolution of the peculiar trophic ecology of vampire snails.

show abstract

“…2014 ; Yalpani et al. 2017 ) and in the fungal sphingomyelin-binding/toxic proteins nakanori ( Makino et al. 2017 ) and pleurotolysin ( Lukoyanova et al.…”

Section: Resultsmentioning

confidence: 99%

Piercing Fishes: Porin Expansion and Adaptation to Hematophagy in the Vampire Snail Cumia reticulata

Gerdol

Cervelli

Oliverio

et al. 2018

Molecular Biology and Evolution

View full text Add to dashboard Cite

show abstract

“…Previous structural studies of SM-bound sensor proteins did not reveal cholesterol-induced changes in SM conformation since they focused on lysenin (De Colibus et al, 2012) and sticholysin (Mancheñ o et al, 2003), both of which do not require cholesterol for binding SM-containing membranes ( Figure 1B). There have also been elegant structural studies of nakanori (Makino et al, 2017) and pleurotolysin A (Lukoyanova et al, 2015), two proteins that may discriminate between free and cholesterol-bound SM in a manner similar to OlyA. Unfortunately, these earlier studies did not contain bound lipids in their reported structures.…”

Section: Discussionmentioning

confidence: 99%

“…We speculated that there may be other toxins that have the opposite ability: to bind SM-sequestered but not accessible cholesterol. A literature search identified several candidate SM-binding toxins, some of which had been reported to also require cholesterol to bind membranes (Anderluh and Macek, 2002;Bernheimer and Avigad, 1979;Bhat et al, 2013;Makino et al, 2017;Sko caj et al, 2014;Tomita et al, 2004;Yamaji et al, 1998). We overexpressed and purified three toxins from this group, namely lysenin (Lys), equinatoxin II (Eqt), and ostreolysin A (OlyA), for analysis of their respective lipid specificities ( Figure 1A).…”

Section: Olya Senses Sm/cholesterol Complexes In Membranesmentioning

confidence: 99%

Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes

Endapally

Frias

Grzemska

et al. 2019

Cell

116

187

View full text Add to dashboard Cite

Graphical Abstract Highlights d OlyA detects sphingomyelin/cholesterol complexes but not free sphingomyelin d A shallow channel in OlyA binds ceramide, but not glycerol, phospholipid backbones d OlyA's cholesterol specificity is determined by a single glutamic acid residue d Plasma membranes maintain constant levels of sphingomyelin/cholesterol complexes SUMMARYSphingomyelin and cholesterol are essential lipids that are enriched in plasma membranes of animal cells, where they interact to regulate membrane properties and many intracellular signaling processes. Despite intense study, the interaction between these lipids in membranes is not well understood. Here, structural and biochemical analyses of ostreolysin A (OlyA), a protein that binds to membranes only when they contain both sphingomyelin and cholesterol, reveal that sphingomyelin adopts two distinct conformations in membranes when cholesterol is present. One conformation, bound by OlyA, is induced by stoichiometric, exothermic interactions with cholesterol, properties that are consistent with sphingomyelin/cholesterol complexes. In its second conformation, sphingomyelin is free from cholesterol and does not bind OlyA. A point mutation abolishes OlyA's ability to discriminate between these two conformations. In cells, levels of sphingomyelin/cholesterol complexes are held constant over a wide range of plasma membrane cholesterol concentrations, enabling precise regulation of the chemical activity of cholesterol.

show abstract

“…Lysenin, a protein isolated from the earthworm Eisenia foetida , binds to sphingomyelin with high specificity [62]. On the other end of the spectrum, Nakanori, a protein recently isolated from a non-edible mushroom, was found to bind to both cholesterol and sphingomyelin [63]. Many of these proteins can be fluorescently conjugated and thereby are thus extremely useful in studying various membrane properties.…”

Section: Introduction1mentioning

confidence: 99%

Dynamic pattern generation in cell membranes: Current insights into membrane organization

Raghunathan¹,

Kenworthy²

2018

Biochimica et Biophysica Acta (BBA) - Biomembranes

View full text Add to dashboard Cite

It has been two decades since the lipid raft hypothesis was first presented. Even today, whether these nanoscale cholesterol-rich domains are present in cell membranes is not completely resolved. However, especially in the last few years, a rich body of literature has demonstrated both the presence and the importance of non-random distribution of biomolecules on the membrane, which is the focus of this review. These new developments have pushed the experimental limits of detection and have brought us closer to observing lipid domains in the plasma membrane of live cells. Characterization of biomolecules associated with lipid rafts has revealed a deep connection between biological regulation and function and membrane compositional heterogeneities. Finally, tantalizing new developments in the field have demonstrated that lipid domains might not just be associated with the plasma membrane of eukaryotes but could potentially be a ubiquitous membrane-organizing principle in several other biological systems. This article is part of a Special Issue entitled: Emergence of Complex Behavior in Biomembranes edited by Marjorie Longo.

show abstract

A novel sphingomyelin/cholesterol domain‐specific probe reveals the dynamics of the membrane domains during virus release and in Niemann‐Pick type C

Cited by 38 publications

References 106 publications

Piercing Fishes: Porin Expansion and Adaptation to Hematophagy in the Vampire Snail Cumia reticulata

Piercing Fishes: Porin Expansion and Adaptation to Hematophagy in the Vampire Snail Cumia reticulata

Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes

Dynamic pattern generation in cell membranes: Current insights into membrane organization

Contact Info

Product

Resources

About