Caveolin-1 in cell polarization and directional migration

Grande-García, A.; Pozo, Miguel Á. del

doi:10.1016/j.ejcb.2008.02.001

Cited by 81 publications

(63 citation statements)

References 52 publications

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“…Multiple signaling cascades have been shown to be regulated by the localization of key cascade elements in caveolae membrane microenvironments. Caveolae compartmentalize intracellular signaling pathways to orchestrate tumor metastasis [32,33]. Our findings indicated that the inte- grality of caveolar domains containing P-gp/PrP c clusters is essential to both EGFR transactivation and CD147 up-regulation and, therefore, paclitaxelrelated cancer invasion.…”

Section: Discussionmentioning

confidence: 90%

The role of P-glycoprotein/cellular prion protein interaction in multidrug-resistant breast cancer cells treated with paclitaxel

Cao

et al. 2008

Cell. Mol. Life Sci.

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We previously reported that treatment with P-glycoprotein (P-gp) substrates promotes in vitro invasion in multidrug-resistant (MDR) breast cancer cells. This effect is initiated by the P-gp pump function and mediated by interaction of P-gp with some unknown component(s). However, the underlying mechanism(s) remains poorly understood. Here we confirm a novel physical interaction between P-gp and cellular prion protein (PrP(c)). Blocking P-gp activity or depletion of PrP(c) inhibited paclitaxel (P-gp substrate)- induced invasion. Paclitaxel further facilitated the formation of P-gp/PrP(c) clusters residing in caveolar domains and promoted the association of P-gp with caveolin-1. Both caveolin-1 and the integrity of caveolae were required for the drug-induced invasion. In addition, the P-gp/PrP(c) complex also played an important role in anti-apoptotic activity of MCF7/Adr cells.These data provide new insights into the mode by which MDR breast cancers evade cytotoxic attacks from P-gp substrates and also suggest a role for P-gp/ PrP(c) interaction in this process.

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Section: Discussionmentioning

confidence: 90%

The role of P-glycoprotein/cellular prion protein interaction in multidrug-resistant breast cancer cells treated with paclitaxel

Cao

et al. 2008

Cell. Mol. Life Sci.

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“…Histological staining Previous studies have mentioned the importance of lipids during cell polarization, particularly during cell migration [26,27], but none have been capable of breaking down the composition and rearrangements of these components during the polarization of intact cells. For comparison with commonplace histological methods, samples were dual-labeled for lipid content using the histological stain Oil Red O and for the nucleus using DAPI.…”

Section: Resultsmentioning

confidence: 99%

“…Caveolae are thought to be involved in cell migration from their oriented distribution [6,26] to assist with directional sensing of basal and granular layers of the epidermis during polarization [33]. Caveolar bulbs are also known to localize in the trailing edge of migrating endothelial cells, while cells migrating in 3-D display caveolar bulbs in a soluble, cytoplasmic form in the leading cell edges [6].…”

Section: Ters Studiesmentioning

confidence: 98%

Label-free in vitro visualization and characterization of caveolar bulbs during stimulated re-epithelialization

2014

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Tip-enhanced Raman scattering (TERS) was paired with real-time reverse transcription quantitative polymerase chain reaction (RT-qPCR) to characterize lipid aggregates during stimulated re-epithelialization using an in vitro wound healing model. In this study, lipid fluctuations in the plasma membrane of epidermal keratinocytes were studied at multiple time points post-wounding. TERS measurements for the first time were also combined with sample analysis after initial wounding and 24 h of wound healing. This enabled simultaneous visualization and characterization of caveolar bulb distribution during wound healing stages, providing noninvasive insight into their associated lipid structure and coating protein, caveolin, in the nanometer range. The combination of Raman spectroscopy and scanning probe microscopy in TERS gives access to topographic and chemical structure information in a single experiment. It is the intrinsic specificity and sensitivity of TERS that enable this discrete detection of cell surface components on the nanometer scale. In contrast with competing biochemical methods, the applied technique does not interfere with the cellular composition, enabling lipid structure analysis without digestion or detergents, and displayed great potential for future biological in vivo studies.

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“…CAV1 is an integral membrane protein, originally identified as one of the main tyrosine-phosphorylated substrates in v-src-transformed fibroblasts. CAV1 contains a scaffolding domain (CSD) of 20 amino acids that interacts with different proteins, such as G-protein-coupled receptors, G proteins, endothelial nitric oxide synthase (eNOS), and Rho proteins including CDC42 (Head & Insel 2007, Grande-Garcia & del Pozo 2008. These interactions led to the 'caveolin signaling hypothesis' (Head & Insel 2007), in which CAV1 may act as a specialized PM structure able to assemble and coordinate the functions of multiple complexes involved in signal transduction, cellular traffic, lipid homeostasis, and cell adhesion (Grande-Garcia & del Pozo 2008).…”

Section: Introductionmentioning

confidence: 99%

“…CAV1 contains a scaffolding domain (CSD) of 20 amino acids that interacts with different proteins, such as G-protein-coupled receptors, G proteins, endothelial nitric oxide synthase (eNOS), and Rho proteins including CDC42 (Head & Insel 2007, Grande-Garcia & del Pozo 2008. These interactions led to the 'caveolin signaling hypothesis' (Head & Insel 2007), in which CAV1 may act as a specialized PM structure able to assemble and coordinate the functions of multiple complexes involved in signal transduction, cellular traffic, lipid homeostasis, and cell adhesion (Grande-Garcia & del Pozo 2008). Although the classic morphology of the omega-shaped invagination of caveolae has not been found in sperm, CAV1 has been observed forming homo-oligomers, which are dissociated during capacitation by cholesterol depletion (Sleight et al 2005).…”

Section: Introductionmentioning

confidence: 99%

The association between CDC42 and caveolin-1 is involved in the regulation of capacitation and acrosome reaction of guinea pig and mouse sperm

Baltiérrez-Hoyos

Roa-Espitia²,

Hernández‐González³

2012

Reproduction

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In the mammalian sperm, the acrosome reaction (AR) is considered to be a regulated secretion that is an essential requirement for physiological fertilization. The AR is the all-or-nothing secretion system that allows for multiple membrane fusion events. It is a Ca 2C -regulated exocytosis reaction that has also been shown to be regulated by several signaling pathways. CDC42 has a central role in the regulated exocytosis through the activation of SNARE proteins and actin polymerization. Furthermore, the lipid raft protein caveolin-1 (CAV1) functions as a scaffold and guanine nucleotide dissociation inhibitor protein for CDC42, which is inactivated when associated with CAV1. CDC42 and other RHO proteins have been shown to localize in the acrosome region of mammalian sperm; however, their relationship with the AR is unknown. Here, we present the first evidence that CDC42 and CAV1 could be involved in the regulation of capacitation and the AR. Our findings show that CDC42 is activated early during capacitation, reaching an activation maximum after 20 min of capacitation. Spontaneous and progesterone-induced ARs were inhibited when sperm were capacitated in presence of secramine A, a specific CDC42 inhibitor. CAV1 and CDC42 were co-immunoprecipitated from the membranes of noncapacitated sperm; this association was reduced in capacitated sperm, and our data suggest that the phosphorylation (Tyr14) of CAV1 by c-Src is involved in such reductions. We suggest that CDC42 activation is favored by the disruption of the CAV1-CDC42 interaction, allowing for its participation in the regulation of capacitation and the AR.

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Caveolin-1 in cell polarization and directional migration

Cited by 81 publications

References 52 publications

The role of P-glycoprotein/cellular prion protein interaction in multidrug-resistant breast cancer cells treated with paclitaxel

The role of P-glycoprotein/cellular prion protein interaction in multidrug-resistant breast cancer cells treated with paclitaxel

Label-free in vitro visualization and characterization of caveolar bulbs during stimulated re-epithelialization

The association between CDC42 and caveolin-1 is involved in the regulation of capacitation and acrosome reaction of guinea pig and mouse sperm

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