The caveolae dress code: structure and signaling

Lamaze, Christophe; Tardif, Nicolas; Dewulf, Melissa; Vassilopoulos, Stéphane; Blouin, Cédric M.

doi:10.1016/j.ceb.2017.02.014

Cited by 131 publications

(123 citation statements)

References 109 publications

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“…However, although newer studies actually revealed that blocking clathrin-dependent uptake can induce increase in clathrin-independent endocytosis (Damke et al 1995), the finding that both potassium depletion and acidification of the cytosol inhibited uptake of ricin by about 50% fits nicely with the large capacity of the Cdc42-dependent pathway (Howes et al 2010b). When it comes to the question of the role of caveolae in endocytosis, this has been debated for decades (Hommelgaard et al 2005; Sandvig et al 2008; van Deurs et al 1993; Lamaze et al 2017; Cheng et al 2010; Sharma et al 2004), and a more detailed discussion of caveolae and their role in endocytosis can be found below. It was in fact not until it was published that the dynamin mutant K44A inhibited clathrin-dependent endocytosis without blocking fluid phase uptake that it was generally accepted that there are different endocytic mechanisms (Damke et al 1994).…”

Section: Introductionmentioning

confidence: 99%

“…Caveolae have been reported to be important for uptake of albumin in endothelial cells (Schnitzer et al 1994), and the possibility exists that there are different types of caveolae with specialized functions as for instance dynamin-2 is not found in all caveolae (Lamaze et al 2017). Caveolae are today, at least in most cells, considered as quite stable membrane structures (van Deurs et al 2003; Pelkmans et al 2004; Parton et al 2006; Kirkham et al 2005) with a role in signaling and in providing membrane during stretching of the plasma membrane (Bastiani and Parton 2010).…”

Section: Introductionmentioning

confidence: 99%

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Clathrin-independent endocytosis: an increasing degree of complexity

Sandvig

Kavaliauskiene

Skotland

2018

Histochem Cell Biol

163

177

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This article aims at providing an update on the complexity of clathrin-independent endocytosis. It is now almost 30 years since we first wrote a review about its existence; at that time many people believed that with the exception of macropinocytosis, which will only be briefly mentioned in this review, all uptake could be accounted for by clathrin-dependent endocytosis. Now it is generally accepted that there are different clathrin-independent mechanisms, some of them regulated by ligands and membrane lipid composition. They can be both dynamin-dependent and -independent, meaning that the uptake cannot be accounted for by caveolae and other dynamin-dependent processes such as tubular structures that can be induced by toxins, e.g. Shiga toxin, or the fast endophilin mediated endocytosis recently described. Caveolae seem to be mostly quite stable structures with other functions than endocytosis, but evidence suggests that they may have cell-type dependent functions. Although several groups have been working on endocytic mechanisms for years, and new advanced methods have improved our ability to study mechanistic details, there are still a number of important questions we need to address, such as: How many endocytic mechanisms does a cell have? How quantitatively important are they? What about the complexity in polarized cells where clathrin-independent endocytosis is differentially regulated on the apical and basolateral poles? These questions are not easy to answer since one and the same molecule may contribute to more than one process, and manipulating one mechanism can affect another. Also, several inhibitors of endocytic processes commonly used turn out to be less specific than originally thought. We will here describe the current view of clathrin-independent endocytic processes and the challenges in studying them.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Clathrin-independent endocytosis: an increasing degree of complexity

Sandvig

Kavaliauskiene

Skotland

2018

Histochem Cell Biol

163

177

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“…Despite their discovery almost 70 years ago, the molecular details of the composition and assembly of these structures have only recently begun to emerge (1,2). Caveolin proteins Cav1, Cav2, and Cav3 are the core components of caveolae.…”

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confidence: 99%

“…The core protein Cav1 has been observed to bind to phosphatidylserine (PtdSer) 2 in vitro and also interacts with other anionic lipids such as phosphatidylinositol 4,5-bisphosphate (PtdIns (4,5)P 2 ) (3, 4). Likewise, cavin1 can bind PtdSer in vitro with high affinity and specificity (5).…”

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confidence: 99%

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Spelunking for lipids in caveolae

Field

2017

Journal of Biological Chemistry

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Edited by Dennis R. Voelker Phosphatidylserine (PtdSer) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2 ) have been implicated in the maintenance of caveolae, but direct evidence that these lipids are required for normal caveolar structure and dynamics in living cells has been lacking. A new study by Fairn and colleagues uses sophisticated tools to perturb specific lipids in living cells to assess the consequences for caveolae. This study demonstrates disparate roles for these lipids in the stability and mobility of caveolae and points the way for future work to understand how these lipids contribute to the biology of caveolae.

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Lung Endothelial Transcytosis

Jones

Minshall

2020

Comprehensive Physiology

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The caveolae dress code: structure and signaling

Cited by 131 publications

References 109 publications

Clathrin-independent endocytosis: an increasing degree of complexity

Clathrin-independent endocytosis: an increasing degree of complexity

Spelunking for lipids in caveolae

Lung Endothelial Transcytosis

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