Membrane mechanisms for signal transduction: The coupling of the meso-scale raft domains to membrane-skeleton-induced compartments and dynamic protein complexes

Kusumi, Akihiro; Fujiwara, Takeshi; Morone, Nobuhiro; Yoshida, Kenta; Chadda, Rahul; Xie, Min; Kasai, Rinshi S.; Suzuki, Kenichi

doi:10.1016/j.semcdb.2012.01.018

Cited by 130 publications

(114 citation statements)

References 189 publications

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“…The N-glycans on extracellular domains are often hundreds of Ångstroms above the plasma membrane, where the galectin lattice extends laterally (see poster). The plasma membrane is also compartmentalized by lipid microdomains (or rafts) and the submembranous cytoskeleton into nanoscale compartments (Kusumi et al, 2012). The galectin lattice represents an additional layer of membrane organization that controls diffusion, complex formation and domain interactions in the plasma membrane (Lajoie et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

The galectin lattice at a glance

Nabi

Shankar

Dennis

2015

Journal of Cell Science

252

222

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Galectins are a family of widely expressed β-galactoside-binding lectins in metazoans. The 15 mammalian galectins have either one or two conserved carbohydrate recognition domains (CRDs), with galectin-3 being able to pentamerize; they form complexes that crosslink glycosylated ligands to form a dynamic lattice. The galectin lattice regulates the diffusion, compartmentalization and endocytosis of plasma membrane glycoproteins and glycolipids. The galectin lattice also regulates the selection, activation and arrest of T cells, receptor kinase signaling and the functionality of membrane receptors, including the glucagon receptor, glucose and amino acid transporters, cadherins and integrins. The affinity of transmembrane glycoproteins to the galectin lattice is proportional to the number and branching of their N-glycans; with branching being mediated by Golgi N-acetylglucosaminyltransferasebranching enzymes and the supply of UDP-GlcNAc through metabolite flux through the hexosamine biosynthesis pathway. The relative affinities of glycoproteins for the galectin lattice depend on the activities of the Golgi enzymes that generate the epitopes of their ligands and, thus, provide a means to analyze biological function of lectins and of the 'glycome' more broadly.

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Section: Introductionmentioning

confidence: 99%

The galectin lattice at a glance

Nabi

Shankar

Dennis

2015

Journal of Cell Science

252

222

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“…Actually, molecules located within 200-300 nm from the probed molecule were labeled by the EMARS reaction (4). This distance corresponds to the size of lipid rafts on stimulation (1,2). …”

Section: B the Emars Methodsmentioning

confidence: 99%

“…The size of membrane microdomains such as lipid rafts varies depending on cell types and with or without a variety of stimulation (1,2). From this viewpoint, EMARS methods for microdomains of various sizes would be desired.…”

Section: H Conclusion and Perspectivementioning

confidence: 99%

“…in cholesterol, (glyco) sphingolipids, glycosylphosphatidylinositol (GPI)-anchored proteins, and Src-family kinases, are on a small scale of less than 20 nm in resting cells, but they become on a large scale of more than 100 nm upon stimulation such as binding of growth factors and other ligands (1,2).…”

mentioning

confidence: 99%

“…Morphological visualization with fluorescence microscopy or electron microscopy is reliable in that co-localization of distinct molecules is directly observed under physiological conditions. Especially, single molecule tracking technology allows us to visualize the real-time movement of molecular assemblies under living conditions (2). However, testing molecules must be known before performing such experiments.…”

mentioning

confidence: 99%

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Segregation of Lipid Rafts Revealed by the EMARS Method Using GPI-Anchored HRP Fusion Proteins

Miyagawa-Yamaguchi

Kotani

Honke

2014

TIGG

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Lipid rafts serve as a platform for important biological events such as signal transduction, cell adhesion, and protein trafficking. To elucidate the molecular mechanisms of these events, identification of interacting molecules in individual raft domains is required. We have developed a novel method termed enzymemediated activation of radical source (EMARS), by which molecules in the vicinity within 300 nm from horseradish peroxidase (HRP) set on the probed molecule are labeled. Recently, we have established a new version of the EMARS system, in which the EMARS reaction is catalyzed by HRP expressed by genetic engineering. In order to express HRP in lipid rafts, HRP was constructed as a GPI-anchored form (HRP-GPI). Two kinds of HRP-GPIs, in which GPI attachment signals of human decay accelerating factor and Thy-1 were separately connected to the Cterminus of HRP, were expressed in human HeLa S3 cells, and the EMARS reaction was catalyzed by these expressed HRP-GPIs under a living condition. As a result, these HRP-GPIs underwent different N-glycosylation and formed distinct molecular clusters.Thus, this novel approach is able to identify molecular clusters associated with particular GPI-anchored proteins, suggesting that it can segregate individual lipid raft domains.

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Tiki proteins are glycosylphosphatidylinositol‐anchored proteases

Zheng

Zhang

2022

FEBS Letters

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Wnt signalling pathways play pivotal roles in development, homeostasis and human diseases, and are tightly regulated. We previously identified Tiki as a novel family of Wnt inhibitory proteases. Tiki proteins were predicted as type I transmembrane proteins and can act in both Wnt‐producing and Wnt‐responsive cells. Here, we characterize Tiki proteins as glycosylphosphatidylinositol (GPI)‐anchored proteases. TIKI1/2 proteins are enriched on the detergent‐resistant membrane microdomains and can be released from the plasma membrane by GPI‐specific glycerophosphodiesterases GDE3 and GDE6, but not by GDE2. The GPI anchor determines the cellular localization of Tiki proteins and their regulation by GDEs, but not their inhibitory activity on Wnt signalling. Our study uncovered novel characteristics and potential regulations of the Tiki family proteases.

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Membrane mechanisms for signal transduction: The coupling of the meso-scale raft domains to membrane-skeleton-induced compartments and dynamic protein complexes

Cited by 130 publications

References 189 publications

The galectin lattice at a glance

The galectin lattice at a glance

Segregation of Lipid Rafts Revealed by the EMARS Method Using GPI-Anchored HRP Fusion Proteins

Tiki proteins are glycosylphosphatidylinositol‐anchored proteases

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