Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin

Stoeber, Miriam; Stoeck, Ina Karen; Hänni, Christine; Bleck, Christopher K. E.; Balistreri, Giuseppe; Helenius, Ari

doi:10.1038/emboj.2012.98

Cited by 151 publications

(208 citation statements)

References 58 publications

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“…The results showed that the average duration time of caveolae was decreased in cells depleted of EHD2, whereas the lateral displacement length was significantly increased (Fig. 7C,D), which nicely corresponds with previous work showing that EHD2 stabilise caveolae at the cell surface (Morén et al, 2012;Stoeber et al, 2012). Interestingly, the mean duration time of caveolae was increased in cells lacking cavin3, whereas the lateral movement was similar to that in control cells (Fig.…”

Section: Cavin3 Is Preferentially Associated With Deeply Invaginatedsupporting

confidence: 90%

“…they are composed of a fixed number of molecules and can exist in different states) in need of strict control. The dimeric ATPase EH-domain containing 2 (EHD2) forms oligomeric rings around lipid membranes and has been shown to interact with caveolae components and localise to the neck of caveolae to stabilise these structures at the cell surface (Morén et al, 2012;Stoeber et al, 2012). Previously, specific kinases were shown to effect such fission and fusion of caveolae , and following osmotic shock or mechanic stress, caveolae have been proposed to flatten out or be released from the membrane in order to cope with sudden changes in membrane tension (Nassoy and Lamaze, 2012;Sinha et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

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Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of caveolae

Mohan

Morén

Larsson

et al. 2015

Journal of Cell Science

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Caveolae are invaginations of the cell surface thought to regulate membrane tension, signalling, adhesion and lipid homeostasis owing to their dynamic behaviour ranging from stable surface association to dynamic rounds of fission and fusion with the plasma membrane. The caveolae coat is generated by oligomerisation of the membrane protein caveolin and the family of cavin proteins. Here, we show that cavin3 (also known as PRKCDBP) is targeted to caveolae by cavin1 (also known as PTRF) where it interacts with the scaffolding domain of caveolin1 and promote caveolae dynamics. We found that the N-terminal region of cavin3 binds a trimer of the cavin1 N-terminus in competition with a homologous cavin2 (also known as SDPR) region, showing that the cavins form distinct subcomplexes through their N-terminal regions. Our data shows that cavin3 is enriched at deeply invaginated caveolae and that loss of cavin3 in cells results in an increase of stable caveolae and a decrease of caveolae that are only present at the membrane for a short time. We propose that cavin3 is recruited to the caveolae coat by cavin1 to interact with caveolin1 and regulate the duration time of caveolae at the plasma membrane.

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Section: Cavin3 Is Preferentially Associated With Deeply Invaginatedsupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of caveolae

Mohan

Morén

Larsson

et al. 2015

Journal of Cell Science

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“…[31] EHD2 is an ATPase, present at the neck of caveolae. [50][51][52] EHD2 is not required for caveolae formation but stabilizes the caveolae at the plasma membrane. EHD2 depletion results in increased Cav mobility and caveolae endocytosis.…”

Section: The Caveolae Structurementioning

confidence: 99%

Caveolae and cancer: A new mechanical perspective

Lamaze¹,

Torrino²

2015

Biomed J

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“…Cavin-3 promotes caveolae dynamics [79] and absence of cavin-3 leads to less trafficking of caveolae derived vesicles along microtubules [82]. On the contrary, the caveolae associated protein EH-domain containing protein 2 (EHD2) stabilizes caveolae at the plasma membrane by linking it to actin [83,84].…”

Section: The Cavinesmentioning

confidence: 99%

Human Adipocytes : Proteomic Approaches

Jufvas¹

2016

Linköping University Medical Dissertations

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Type 2 diabetes is characterized by increased levels of glucose in the blood originating from insulin resistance in insulin sensitive tissues and from reduced pancreatic insulin production. Around 400 million people in the world are diagnosed with type 2 diabetes and the correlation with obesity is strong. In addition to life style induction of obesity and type 2 diabetes, there are indications of genetic and epigenetic influences. This thesis has focused on the characterization of primary human adipocytes, who play a crucial role in the development of type 2 diabetes. Histones are important proteins in chromatin dynamics and may be one of the factors behind epigenetic inheritance. In paper I, we characterized histone variants and posttranslational modifications in human adipocytes. Several of the specific posttranslational histone modifications we identified have been characterized in other cell types, but the majority was not previously known. Moreover, we identified a variant of histone H4 on protein level for the first time. In paper II, we studied specific histone H3 methylations in the adipocytes. We found that overweight is correlated with a reduction of H3K4me2 while type 2 diabetes is associated with an increase of H3K4me3. This shows a genome-wide difference in important chromatin modifications that could help explain the epidemiologically shown association between epigenetics and metabolic health. Caveolae is a plasma membrane structure involved in the initial and important steps of insulin signaling. In paper III we characterized the IQGAP1 interactome in human adipocytes and suggest that IQGAP1 is a link between caveolae and the cytoskeleton. Moreover, the amount of IQGAP1 is drastically lower in adipocytes from type 2 diabetic subjects compared with controls implying a potential role for IQGAP1 in insulin resistance. In conclusion, this thesis provides new insights into the insulin signaling frameworks and the histone variants and modifications of human adipocytes

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Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin

Cited by 151 publications

References 58 publications

Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of caveolae

Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of caveolae

Caveolae and cancer: A new mechanical perspective

Human Adipocytes : Proteomic Approaches

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