In recent years, the single flagellum of T. brucei has been demonstrated as an essential and multifunctional organelle with critical roles in motility, host cell attachment, sensory perception, cell morphogenesis, cell division and host-parasite interaction. In addition, recent studies have revealed that the flagellar motility is required for the viability of both the insect-form and the bloodstream-form T. brucei, suggesting that flagellar function analysis may uncover potential novel drug targets. Though many studies have revealed the multifunctional nature of the trypanosome flagellum as stated above, the underlying molecular mechanisms are still unclear and the component of the flagellar proteome needs to be identified. As we know, flagellar proteins are all nucleus-encoded, initially synthesized in cytoplasm and then transported to the flagellum. In the past decade, a variety of computational methods have been developed for predicting protein subcellular localization. However, most of the existing tools focus on proteins targeted to major locations such as endoplasmic reticulum, mitochondria, nucleus, and so on. These tools do not provide any information on proteins targeted to more specialized organelles like flagellum. To the best of our knowledge, only a few methods provide predictions for flagellar proteins in prokaryotes. Moreover, no similar prediction tools are available for eukaryotic flagellar proteins. Flagellum is a relatively “closed” organelle and can best be compared with the nucleus considering the entry and exit activities. Though the flagellar membranes are contiguous with the plasma membrane, they are functionally distinct membrane domains with distinct composition and biochemical properties. Therefore, there must be specific targeting and importing mechanisms for flagellar proteins, which are still unknown. Recent proteomic studies have revealed a large number of flagellar proteins in trypanosomes, greatly expanding the inventory of known flagellar proteins. However, due to technical limitations for purification of the intact flagellum from T. brucei, a lot of flagellar proteins fail to be detected and many detected proteins can not be assigned to flagellum with certainty. In this study, we developed a computational method TFPP to identify flagellar proteins in T. brucei based on sequence-derived features. We collected a set of flagellar and non-flagellar proteins that have been annotated with high confidence, and selected a number of discriminating properties from various sequence and structural features using a feature selection procedure. Tumor metastasis is a complex event involving multiple steps including separation of cancer cells from the compact primary tumor, migration into vessels, invasion in tissue and formation of a secondary tumor nodule. Although still under debate, epithelial to mesenchymal transition seems to be one of the key events in local progress and metastasis of epithelial malignancies. EMT is a complex multistep event, which changes not only cell morphology but also enables cells to gain important new functions like the expression of new molecules or migration and invasion. In addition to morphological changes, the process of EMT is characterized by differences in transcription and expression of epithelial and mesenchymal genes. One of the most important molecular markers of epithelial cells is the epithelial adhesion molecule E-cadherin, mediating cell-cell interactions.

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