A. F. G. Quest, L. Lobos-Gonzalez, S. Nunez, C. Sanhueza, J.-G. Fernandez, A. Aguirre, D. Rodriguez, L. Leyton and V. Torres Pages 266 - 281 ( 16 )
Caveolins are a family of membrane proteins required for the formation of small plasma membrane invaginations called caveolae that are implicated in cellular trafficking processes. In addition to this structural role, these scaffolding proteins modulate numerous intracellular signaling pathways; often via direct interaction with specific binding partners. Caveolin-1 is particularly well-studied in this respect and has been attributed a large variety of functions. Thus, Caveolin-1 also represents the best-characterized isoform of this family with respect to its participation in cancer. Rather strikingly, available evidence indicates that Caveolin-1 belongs to a select group of proteins that function, depending on the cellular settings, both as tumor suppressor and promoter of cellular traits commonly associated with enhanced malignant behavior, such as metastasis and multi-drug resistance. The mechanisms underlying such ambiguity in Caveolin-1 function constitute an area of great interest. Here, we will focus on discussing how Caveolin-1 modulates cell death and survival pathways and how this may contribute to a better understanding of the ambiguous role this protein plays in cancer.
Caveolin-1, cell death, metastasis, multi-drug resistance, proliferation, tumor suppression, caveolae, oligomerization, biogenesis, cavins, vesicle trafficking, endocytosis, cholesterol homeostasis, signal transduction, gene expression.
Laboratorio de Comunicaciones Celulares, Centro de Estudios Moleculares de la Celula (CEMC), Facultad de Medicina, Universidad de Chile, Av. Independencia 1027, Santiago, Chile.