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Review
. 2012 Jun;14(6):679-88.
doi: 10.1093/neuonc/nos079. Epub 2012 Apr 16.

Caveolin-1, caveolae, and glioblastoma

Marie-Odile Parat  1 , Gregory J Riggins
Affiliations
Review

Caveolin-1, caveolae, and glioblastoma

Marie-Odile Parat et al. Neuro Oncol. 2012 Jun.

Abstract

Glioblastoma multiforme (GBM) is the most common malignant brain tumor and is characterized by high invasiveness, poor prognosis, and limited therapeutic options. Biochemical and morphological experiments have shown the presence of caveolae in glioblastoma cells. Caveolae are flask-shaped plasma membrane subdomains that play trafficking, mechanosensing, and signaling roles. Caveolin-1 is a membrane protein that participates in the formation of caveolae and binds a multitude of signaling proteins, compartmentalizing them in caveolae and often directly regulating their activity via binding to its scaffolding domain. Caveolin-1 has been proposed to behave either as a tumor suppressor or as an ongogene depending on the tumor type and progress. This review discusses the existing information on the expression and function of caveolin-1 and caveolae in GBM and the role of this organelle and its defining protein on cellular signaling, growth, and invasiveness of GBM. We further analyze the available data suggesting caveolin-1 could be a target in GBM therapy.

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Figures

Fig. 1.
Fig. 1.
Multiple signaling pathways essential to GBM growth and invasion are controlled by caveolin-1. Receptor tyrosine kinases (EGFR), integrins, and uPA are concentrated in caveolae and interact with caveolin-1. Downstream signaling is initiated in caveolae. Caveolin-1 undergoes Src family kinase-mediated tyrosine phosphorylation upon EGF stimulation or integrin engagement. Caveolae endocytosis further controls EGFR presence at the cell surface. Binding to the caveolin-1 scaffolding domain inhibits and sequesters EGFR, as well as MT-1 MMP in caveolae. Caveolin-1 also directly inhibits MEK-1 and ERK-2 downstream of the EGFR activation. UPA forms a complex with integrins and caveolin-1 that signals through Src family kinases and focal adhesion kinase (FAK). Via interacting with the uPA receptor and MT1-MMP, caveolin-1 spatially controls extracellular proteolysis, including growth factor release from the extracellular matrix, and basement membrane degradation.
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