Cellular interactions with the extracellular matrix are important factors in the development and progression of many types of cancer. Originally characterized as a member of the so-called dystrophin-glycoprotein complex in muscle sarcolemma, dystroglycan (DG) is a transmembrane glycoprotein expressed in a wide variety of tissues at the interface between the basement membrane and cell membrane linking the extracellular matrix to the intracellular cytoskeleton.

Prostate cancer is a main urological disease associated with significant morbidity and mortality. Radical prostatectomy and radiotherapy are potentially curative for localized prostate cancer, while androgen deprivation therapy is the initial systemic therapy for metastatic prostate disease. However, despite temporary response, most patients relapse and evolve into castration resistant cancer.Epithelial-mesenchymal transition (EMT) is a complex gradual process that occurs during embryonic development and/or tumor progression. During this process, cells lose their epithelial characteristics and acquire mesenchymal features. Increasing evidences indicate that EMT promotes prostate cancer metastatic progression and it is closely correlated with increased stemness and drug resistance.In this review, we discuss the main molecular events that directly or indirectly govern the EMT program in prostate cancer, in order to better define the role and the mechanisms underlying this process in prostate cancer progression and therapeutic resistance.

The pRb family proteins (pRb1/105, p107, pRb2/p130), collectively referred to as pocket proteins, are believed to function primarily as regulators of the mammalian cell cycle progression, and suppressors of cellular growth and proliferation. In addition, different studies suggest that these pocket proteins are also involved in development and differentiation of various tissues. Several lines of evidence indicate that generally pRb-family proteins function through their effect on the transcription of E2F-regulated genes. In fact, each of Rb family proteins binds to distinct members of the E2F transcription factors, which regulate the expression of genes whose protein products are necessary for cell proliferation and to drive cell-cycle progression. Nevertheless, pocket proteins can affect the G1/S transition through E2F-independent mechanisms. More recently, a broad range of evidences indicate that pRb-family proteins associate with a wide variety of transcription factors and chromatin remodeling enzymes forming transcriptional repressor complexes that control gene expression. This review focuses on the complex regulatory mechanisms by which pRb-family proteins tell genes when to switch on and off.