2022
DOI: 10.1093/jmcb/mjac066
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Interactive mechanisms between caveolin-1 and actin filaments or vimentin intermediate filaments instruct cell mechanosensing and migration

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Cited by 3 publications
(3 citation statements)
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“…Caveolae also regulate Rho GTPases. The loss of Cav1 impairs actin cytoskeleton equilibrium by the increased phosphorylation of AMPK (AMP-activated protein kinase that regulates small Rho GTPases [ 184 ], and it reduces RhoA-myosin II activation and increases the activity of Rac1/Cdc42-Pak1-cofilin, which results in a decrease in thick actin stress fibers and an increase in lamellipodia [ 10 , 151 , 185 , 186 , 187 ] through the activation of p190RhoGAP [ 10 , 11 , 35 , 188 ]. Caveolar components can also regulate RhoA signaling through other mechanisms, such as the PM targeting of Rac1, physical interactions, and rates of degradation, among others, and therefore influence cytoskeletal regulation [ 10 , 28 , 95 , 189 , 190 ].…”
Section: Interaction Between Caveolae and Cytoskeletonmentioning
confidence: 99%
See 1 more Smart Citation
“…Caveolae also regulate Rho GTPases. The loss of Cav1 impairs actin cytoskeleton equilibrium by the increased phosphorylation of AMPK (AMP-activated protein kinase that regulates small Rho GTPases [ 184 ], and it reduces RhoA-myosin II activation and increases the activity of Rac1/Cdc42-Pak1-cofilin, which results in a decrease in thick actin stress fibers and an increase in lamellipodia [ 10 , 151 , 185 , 186 , 187 ] through the activation of p190RhoGAP [ 10 , 11 , 35 , 188 ]. Caveolar components can also regulate RhoA signaling through other mechanisms, such as the PM targeting of Rac1, physical interactions, and rates of degradation, among others, and therefore influence cytoskeletal regulation [ 10 , 28 , 95 , 189 , 190 ].…”
Section: Interaction Between Caveolae and Cytoskeletonmentioning
confidence: 99%
“…Although there is a cell-dependent regulation of vimentin expression by Cav1 [ 203 , 204 , 205 ], a clear unidirectional regulation of vimentin on Cav1 has been reported. Vimentin depletion facilitates Cav1 mobilization and increases Y14Cav1 phosphorylation [ 187 , 201 , 205 , 206 ]. Finally, regarding IFs type V, which corresponds to the nuclear lamina, the main component of the nucleoskeleton that plays an important role in gene expression regulation and has been described as a link with Cav2.…”
Section: Interaction Between Caveolae and Cytoskeletonmentioning
confidence: 99%
“…The germination of caveolae is regulated by kinase and phosphatase [ 63 ]. Studies have shown that kinase inhibitors can inhibit CavME, and phosphatase inhibitors can enhance CavME, which is caused by the loss of connection between caveolae and actin fibers after the rapid phosphorylation of Filamin A protein that is mediated by protein kinase Cα [ 64 ]. Once caveolae are detached from the plasma membrane, compared with vesicles produced by the CME pathway, vesicles produced by the CavME pathway are more likely to be transported to the Golgi apparatus and endoplasmic reticulum to avoid lysosomes and protect contents from the degradation of hydrolase in lysosomes [ 65 ].…”
Section: Intestinal Cell Pathwaymentioning
confidence: 99%