The Dioxin receptor modulates Caveolin-1 mobilization during directional migration: role of cholesterol
详细信息 查看全文
- 作者：Javier Rey-Barroso ; Alberto Alvarez-Barrientos…
- 关键词：Dioxin receptor ; Caveolin ; 1 ; Membrane microdomains ; Endocytosis ; Cholesterol
- 刊名：Cell Communication and Signaling
- 出版年：2014
- 出版时间：December 2014
- 年：2014
- 卷：12
- 期：1
- 全文大小：3,025 KB
- 参考文献：1. Nebert, DW, Dalton, TP, Okey, AB, Gonzalez, FJ (2004) Role of aryl hydrocarbon receptor-mediated induction of the CYP1 enzymes in environmental toxicity and cancer. J Biol Chem 279: pp. 23847-23850 CrossRef
2. Shimizu, Y, Nakatsuru, Y, Ichinose, M, Takahashi, Y, Kume, H, Mimura, J, Fujii-Kuriyama, Y, Ishikawa, T (2000) Benzo[a]pyrene carcinogenicity is lost in mice lacking the aryl hydrocarbon receptor. Proc Natl Acad Sci U S A 97: pp. 779-782 CrossRef
3. Pohjanvirta, R (2012) The AH receptor in Biology and Toxicology. John Wiley & Sons, New York
4. Sauzeau, V, Carvajal-Gonzalez, JM, Riolobos, AS, Sevilla, MA, Menacho-Marquez, M, Roman, AC, Abad, A, Montero, MJ, Fernandez-Salguero, P, Bustelo, XR (2011) Transcriptional factor aryl hydrocarbon receptor (Ahr) controls cardiovascular and respiratory functions by regulating the expression of the Vav3 proto-oncogene. J Biol Chem 286: pp. 2896-2909 CrossRef
5. Cho, YC, Zheng, W, Jefcoate, CR (2004) Disruption of cell-cell contact maximally but transiently activates AhR-mediated transcription in 10T1/2 fibroblasts. Toxicol Appl Pharmacol 199: pp. 220-238 CrossRef
6. Sadek, CM, Allen-Hoffmann, BL (1994) Cytochrome P450IA1 is rapidly induced in normal human keratinocytes in the absence of xenobiotics. J Biol Chem 269: pp. 16067-16074
7. Qin, H, Powell-Coffman, JA (2004) The Caenorhabditis elegans aryl hydrocarbon receptor, AHR-1, regulates neuronal development. Dev Biol 270: pp. 64-75 CrossRef
8. Barouki, R, Coumoul, X, Fernandez-Salguero, PM (2007) The aryl hydrocarbon receptor, more than a xenobiotic-interacting protein. FEBS Lett 581: pp. 3608-3615 CrossRef
9. Gomez-Duran, A, Carvajal-Gonzalez, JM, Mulero-Navarro, S, Santiago-Josefat, B, Puga, A, Fernandez-Salguero, PM (2009) Fitting a xenobiotic receptor into cell homeostasis: how the dioxin receptor interacts with TGFbeta signaling. Biochem Pharmacol 77: pp. 700-712 CrossRef
10. Mulero-Navarro, S, Pozo-Guisado, E, Perez-Mancera, PA, Alvarez-Barrientos, A, Catalina-Fernandez, I, Hernandez-Nieto, E, Saenz-Santamaria, J, Martinez, N, Rojas, JM, Sanchez-Garcia, I, Fernandez-Salguero, PM (2005) Immortalized mouse mammary fibroblasts lacking dioxin receptor have impaired tumorigenicity in a subcutaneous mouse xenograft model. J Biol Chem 280: pp. 28731-28741 CrossRef
11. Roman, AC, Carvajal-Gonzalez, JM, Rico-Leo, EM, Fernandez-Salguero, PM (2009) Dioxin receptor deficiency impairs angiogenesis by a mechanism involving VEGF-A depletion in the endothelium and transforming growth factor-beta overexpression in the stroma. J Biol Chem 284: pp. 25135-25148 CrossRef
12. Tomkiewicz, C, Herry, L, Bui, LC, Metayer, C, Bourdeloux, M, Barouki, R, Coumoul, X (2013) The aryl hydrocarbon receptor regulates focal adhesion sites through a non-genomic FAK/Src pathway. Oncogene 32: pp. 1811-1820 CrossRef
13. Diry, M, Tomkiewicz, C, Koehle, C, Coumoul, X, Bock, KW, Barouki, R, Transy, C (2006) Activation of the dioxin/aryl hydrocarbon receptor (AhR) modulates cell plasticity through a JNK-dependent mechanism. Oncogene 25: pp. 5570-5574 CrossRef
14. Carvajal-Gonzalez, JM, Roman, AC, Cerezo-Guisado, MI, Rico-Leo, EM, Martin-Partido, G, Fernandez-Salguero, PM (2009) Loss of dioxin-receptor expression accelerates wound healing in vivo by a mechanism involving TGF{beta}. J Cell Sci 122: pp. 1823-1833 CrossRef
15. Carvajal-Gonzalez, JM, Mulero-Navarro, S, Roman, AC, Sauzeau, V, Merino, JM, Bustelo, XR, Fernandez-Salguero, PM (2009) The dioxin receptor regu - 刊物主题：Cell Biology; Protein-Ligand Interactions; Receptors; Cytokines and Growth Factors;
- 出版者：BioMed Central
- ISSN：1478-811X
文摘
Background Adhesion and migration are relevant physiological functions that must be regulated by the cell under both normal and pathological conditions. The dioxin receptor (AhR) has emerged as a transcription factor regulating both processes in mesenchymal, epithelial and endothelial cells. Indirect results suggest that AhR could cooperate not only with additional transcription factors but also with membrane-associated proteins to drive such processes. Results In this study, we have used immortalized and primary dermal fibroblasts from wild type (AhR+/+) and AhR-null (AhR??/em>) mice to show that AhR modulates membrane distribution and mobilization of caveolin-1 (Cav-1) during directional cell migration. AhR co-immunoprecipitated with Cav-1 and a fraction of both proteins co-localized to detergent-resistant membrane microdomains (DRM). Consistent with a role of AhR in the process, AhR??/em> cells had a significant reduction in Cav-1 in DRMs. Moreover, high cell density reduced AhR nuclear levels and moved Cav-1 from DRMs to the soluble membrane in AhR+/+ but not in AhR??/em> cells. Tyrosine-14 phosphorylation had a complex role in the mechanism since its upregulation reduced Cav-1 in DRMs in both AhR+/+ and AhR??/em>cells, despite the lower basal levels of Y14-Cav-1 in the null cells. Fluorescence recovery after photobleaching revealed that AhR knock-down blocked Cav-1 transport to the plasma membrane, a deficit possibly influencing its depleted levels in DRMs. Membrane distribution of Cav-1 in AhR-null fibroblasts correlated with higher levels of cholesterol and with disrupted membrane microdomains, whereas addition of exogenous cholesterol changed the Cav-1 distribution of AhR+/+ cells to the null phenotype. Consistently, higher cholesterol levels enhanced caveolae-dependent endocytosis in AhR-null cells. Conclusions These results suggest that AhR modulates Cav-1 distribution in migrating cells through the control of cholesterol-enriched membrane microdomains. Our study also supports the likely possibility of membrane-related, transcription factor independent, functions of AhR.