Role of dynamin and clathrin in the cellular trafficking of flotillins

Meister, Melanie; Zuk, Alexandra V.; Tikkanen, Ritva

doi:10.1111/febs.12834

Cited by 23 publications

(20 citation statements)

References 90 publications

(168 reference statements)

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“…Although of potential interest, it is not known whether this flotillin-dependent cadherin recycling mechanism exists in other cell types. It is noteworthy that A431 cells overexpress EGFR and this could affect endocytosis and recycling of cadherin and flotillin (Bryant et al, 2007;Meister et al, 2014). Moreover, we never observed such a mechanism in the cell lines we tested.…”

Section: Flotillin-dependent Regulation Of Cadherin Recyclingmentioning

confidence: 68%

Flotillins in intercellular adhesion – from cellular physiology to human diseases

Bodin

Planchon

Morris

et al. 2014

Journal of Cell Science

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Flotillin 1 and 2 are ubiquitous and highly conserved proteins. They were initially discovered in 1997 as being associated with specific caveolin-independent cholesterol-and glycosphingolipid-enriched membrane microdomains and as being expressed during axon regeneration. Flotillins have a role in a large number of physiopathological processes, mainly through their function in membrane receptor clustering and in the regulation of clathrinindependent endocytosis. In this Commentary, we summarize the research performed so far on the role of flotillins in cell-cell adhesion. Recent studies have demonstrated that flotillins directly regulate the formation of cadherin complexes. Indeed, flotillin microdomains are required for the dynamic association and stabilization of cadherins at cell-cell junctions and also for cadherin signaling. Moreover, because flotillins regulate endocytosis and also the actin cytoskeleton, they could have an indirect role in the assembly and stabilization of cadherin complexes. Because it has also recently been shown that flotillins are overexpressed during neurodegenerative diseases and in human cancers, where their upregulation is associated with metastasis formation and poor prognosis, understanding to what extent flotillin upregulation participates in the development of such pathologies is thus of particular interest, as well as how, at the molecular level, it might affect cell adhesion processes.

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Section: Flotillin-dependent Regulation Of Cadherin Recyclingmentioning

confidence: 68%

Flotillins in intercellular adhesion – from cellular physiology to human diseases

Bodin

Planchon

Morris

et al. 2014

Journal of Cell Science

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“…Flotillin redistribution from the plasma membrane to late endosomes is induced also by incubation with EGF [57,58]. In HeLa cells, this effect involves dynamin [59]. It has been suggested that Fyn-dependent phosphorylation of flotillin 1 (Y160) and flotillin 2 (Y163) induces their endocytosis.…”

Section: Flotillinsmentioning

confidence: 99%

Flotillin membrane domains in cancer

Gauthier-Rouvière

Bodin

Comunale

et al. 2020

Cancer Metastasis Rev

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Flotillins 1 and 2 are two ubiquitous, highly conserved homologous proteins that assemble to form heterotetramers at the cytoplasmic face of the plasma membrane in cholesterol-and sphingolipid-enriched domains. Flotillin heterotetramers can assemble into large oligomers to form molecular scaffolds that regulate the clustering of at the plasma membrane and activity of several receptors. Moreover, flotillins are upregulated in many invasive carcinomas and also in sarcoma, and this is associated with poor prognosis and metastasis formation. When upregulated, flotillins promote plasma membrane invagination and induce an endocytic pathway that allows the targeting of cargo proteins in the late endosomal compartment in which flotillins accumulate. These late endosomes are not degradative, and participate in the recycling and secretion of protein cargos. The cargos of this Upregulated Flotillin-Induced Trafficking (UFIT) pathway include molecules involved in signaling, adhesion, and extracellular matrix remodeling, thus favoring the acquisition of an invasive cellular behavior leading to metastasis formation. Thus, flotillin presence from the plasma membrane to the late endosomal compartment influences the activity, and even modifies the trafficking and fate of key protein cargos, favoring the development of diseases, for instance tumors. This review summarizes the current knowledge on flotillins and their role in cancer development focusing on their function in cellular membrane remodeling and vesicular trafficking regulation.

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“…The lipid raft is also a major source of Ab generation, and the plasma membranes of DNM2-negative neuronal cells have been found with an increase in the concentration of the lipid raft. An increased amount of flotillin-1, a marker of lipid raft, was found to be in the plasma membrane of DNM2-negative neuronal cells, confirming the increased presence of lipid raft (Meister et al, 2014). DNM1 knockout mice show reduced levels of secreted and intracellular levels of Ab in cell cultures.…”

Section: Dynamin In Admentioning

confidence: 62%

Dynamin Functions and Ligands: Classical Mechanisms Behind

2016

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Dynamin is a GTPase that plays a vital role in clathrin-dependent endocytosis and other vesicular trafficking processes by acting as a pair of molecular scissors for newly formed vesicles originating from the plasma membrane. Dynamins and related proteins are important components for the cleavage of clathrin-coated vesicles, phagosomes, and mitochondria. These proteins help in organelle division, viral resistance, and mitochondrial fusion/fission. Dysfunction and mutations in dynamin have been implicated in the pathophysiology of various disorders, such as Alzheimer's disease, Parkinson's disease, Huntington's disease, Charcot-Marie-Tooth disease, heart failure, schizophrenia, epilepsy, cancer, dominant optic atrophy, osteoporosis, and Down's syndrome. This review is an attempt to illustrate the dynamin-related mechanisms involved in the above-mentioned disorders and to help medicinal chemists to design novel dynamin ligands, which could be useful in the treatment of dynamin-related disorders.

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Role of dynamin and clathrin in the cellular trafficking of flotillins

Cited by 23 publications

References 90 publications

Flotillins in intercellular adhesion – from cellular physiology to human diseases

Flotillins in intercellular adhesion – from cellular physiology to human diseases

Flotillin membrane domains in cancer

Dynamin Functions and Ligands: Classical Mechanisms Behind

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