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• W2016121297 abstract "MARKs (MAP/Microtubule-Affinity Regulating Kinases), a kinase family related to the cell polarity PAR-1 proteins, phosphorylate Microtubule-Associated Proteins, causing detachment from microtubules and their disassembly. In contrast to MARK1, MARK2, and MARK3, which exhibit uniform cytoplasmic localization, exogenous MARK4 co-localizes with microtubules, centrosomes, and neurite-like processes of neuroblastoma cells. Of the two known isoforms, MARK4L is candidate for an intriguing role in neoplastic transformation, because its expression is restricted to neural progenitors in brain and reappears relatively pronounced in glioma, being also found highly expressed in hepatocarcinoma cell lines. Conversely, several evidences point to a specialized role of MARK4S in post-mitotic neurons. We have recently showed by immunofluorescence (IF) and Western blot (WB) analyses that the endogenous MARK4L protein co-localizes with centrosomes, the nucleolus and the midbody, and co-stains the aberrant centrosomes observed in glioblastoma. Further evidence dissecting the role of MARK4 isoforms is provided in this study, which shows by IF that both MARK4 isoforms have a centrosome and midbody localization in tumors other than glioma and in different normal cell lines. These data favour the view that MARK4 association with the above structures is neither isoform- nor tumor-specific. By contrast we found that the nucleolar localization is a specific feature of the sole L isoform of MARK4. Co-labelling of the kinase with the nucleolar protein nucleolin was investigated in glioma, breast cancer (MCF7), and leukaemia (Kasumi-I) cell lines, versus their normal cell counterparts, in addition to myoblasts and fibroblasts. IF results indicated that MARK4L accumulates within nucleoli exclusively in tumor cell lines, and WB of the respective nucleolar fractions confirmed this finding. Investigation of MARK4L phosphorylation status in nucleoli isolated from glioma versus normal glial cells is in progress, as well as experiments of RNA depletion and proteasome inhibition in nucleoli to determine whether these treatments affect MARK4L retention. Final aim is to gain insight into the determinants required for the nucleolar targeting of MARK4L. Overall, our results reinforce earlier hypothesis of the influence of MARK4 on microtubule, MTOC, and actin-dependent processes, particularly those affecting midbody, and delineate the L isoform as a tumor target through nucleolar association. This study was supported by a grant from the Associazione Italiana per la Ricerca sul Cancro." @default.
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• W2016121297 date "2010-11-01" @default.
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• W2016121297 title "The centrosomal protein MARK4 exhibits specificity of the L isoform through nucleolar association in tumor cell lines" @default.
• W2016121297 doi "https://doi.org/10.1016/j.cancergencyto.2010.07.084" @default.
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