Association and insulin regulated translocation of hormone-sensitive lipase with PTRF

Aboulaich, Nabila; Örtegren, Unn; Vener, Alexander V.; Strålfors, Peter

doi:10.1016/j.bbrc.2006.09.094

Cited by 47 publications

(48 citation statements)

References 16 publications

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“…2 to mass spectrometry, and in addition to what we previously identified by sequencing or by Western blotting, we found cavin [also known as polymerase I and transcript release factor (PTRF) (36)] to be a major constituent, in confirmation of the work of Vinten and colleagues (37,38) in rat adipocytes and that of Aboulaich et al (39,40), who used human fat cells. The role of cavin in caveolae structure/ function remains to be determined, but its relative abundance, its tissue distribution that mirrors that of caveolin-1 and -3 (37,41), and its apparent lack of enzymatic activity (36) suggest a possible structural role, although a functional role in adipocytes has been suggested (40) (see lipid trafficking section below).…”

Section: Caveolae Isolation Protocols and Problemssupporting

confidence: 86%

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Cellular spelunking: exploring adipocyte caveolae

Pilch

Souto

Liu

et al. 2007

Journal of Lipid Research

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It has been known for decades that the adipocyte cell surface is particularly rich in small invaginations we now know to be caveolae. These structures are common to many cell types but are not ubiquitous. They have generated considerable curiosity, as manifested by the numerous publications on the topic that describe various, sometimes contradictory, caveolae functions. Here, we review the field from an "adipocentric" point of view and suggest that caveolae may have a function of particular use for the fat cell, namely the modulation of fatty acid flux across the plasma membrane. Other functions for adipocyte caveolae that have been postulated include participation in signal transduction and membrane trafficking pathways, and it will require further experimental scrutiny to resolve controversies surrounding these possible

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Section: Caveolae Isolation Protocols and Problemssupporting

confidence: 86%

“…4. It was recently suggested that in human adipocytes, cavin/PTRF undergoes insulin-dependent movement from the plasma membrane to the cytosol and nucleus and can interact with hormone-sensitive lipase in the cytosol (40). We have performed similar experiments in rat adipocytes, as shown in Fig.…”

Section: Future Directionsmentioning

confidence: 85%

Cellular spelunking: exploring adipocyte caveolae

Pilch

Souto

Liu

et al. 2007

Journal of Lipid Research

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“…None of these phosphorylation events have yet been linked to caveolae assembly, except for one study that suggests phosphorylation of Cavin1 within DR3 at Ser365 and/or Ser366 can enhance caveolar association (Bai et al, 2011). Likewise, insulin-induced Ser/Thr phosphorylation of Cavin1 is associated with its loss from the plasma membrane (Aboulaich et al, 2011;Aboulaich et al, 2006). However, the precise functional significance of this extensive phosphorylation remains an important unanswered question.…”

Section: The Cavin Family Of Coat Proteinsmentioning

confidence: 99%

Cavin family proteins and the assembly of caveolae

Kovtun

Tillu

Ariotti

et al. 2015

Journal of Cell Science

200

141

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Caveolae are an abundant feature of the plasma membrane in many cells. Until recently, they were generally considered to be membrane invaginations whose formation primarily driven by integral membrane proteins called caveolins. However, the past decade has seen the emergence of the cavin family of peripheral membrane proteins as essential coat components and regulators of caveola biogenesis. In this Commentary, we summarise recent data on the role of cavins in caveola formation, highlighting structural studies that provide new insights into cavin coat assembly. In mammals, there are four cavin family members that associate through homo-and hetero-oligomerisation to form distinct subcomplexes on caveolae, which can be released into the cell in response to stimuli. Studies from several labs have provided a better understanding of cavin stoichiometry and the molecular basis for their oligomerisation, as well as identifying interactions with membrane phospholipids that may be important for caveola function. We propose a model in which coincident, low-affinity electrostatically controlled protein-protein and protein-lipid interactions allow the formation of caveolae, generating a metastable structure that can respond to plasma membrane stress by release of cavins.

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“…The functions of caveolins are closely linked to a family of cytoplasmic proteins termed cavins (Hill et al 2008;Bastiani et al 2009;Hansen et al 2009;McMahon et al 2009). PTRF/ cavin-1 is essential for the formation of caveolae (Hill et al 2008;Liu et al 2008) and, like caveolin, has been shown to be associated with LD function and lipid storage in cultured adipocytes (Aboulaich et al 2006), mice (Liu et al 2008), and human patients (Hayashi et al 2009;Rajab et al 2010). …”

Section: Interactions With Caveolae Caveolins and Cavinsmentioning

confidence: 99%

Not Just Fat: The Structure and Function of the Lipid Droplet

Fujimoto

Parton²

2011

Cold Spring Harbor Perspectives in Biology

408

336

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Lipid droplets (LDs) are independent organelles that are composed of a lipid ester core and a surface phospholipid monolayer. Recent studies have revealed many new proteins, functions, and phenomena associated with LDs. In addition, a number of diseases related to LDs are beginning to be understood at the molecular level. It is now clear that LDs are not an inert store of excess lipids but are dynamically engaged in various cellular functions, some of which are not directly related to lipid metabolism. Compared to conventional membrane organelles, there are still many uncertainties concerning the molecular architecture of LDs and how each function is placed in a structural context. Recent findings and remaining questions are discussed.

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Association and insulin regulated translocation of hormone-sensitive lipase with PTRF

Cited by 47 publications

References 16 publications

Cellular spelunking: exploring adipocyte caveolae

Cellular spelunking: exploring adipocyte caveolae

Cavin family proteins and the assembly of caveolae

Not Just Fat: The Structure and Function of the Lipid Droplet

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