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dc.contributor.authorSalah, Z.
dc.contributor.authorBar-mag, T.
dc.contributor.authorKohn, Y.
dc.contributor.authorPichiorri, F.
dc.contributor.authorPalumbo, T.
dc.contributor.authorMelino, G.
dc.contributor.authorAqeilan, RI
dc.date.accessioned2018-09-16T08:06:08Z
dc.date.available2018-09-16T08:06:08Z
dc.date.issued2013-01-31
dc.identifier.citationCell Death and Disease (2013) 4, e480; doi:10.1038/cddis.2013.6 & 2013 Macmillan Publishers Limited All rights reserved 2041-4889/13en_US
dc.identifier.issn2041-4889
dc.identifier.urihttps://dspace.alquds.edu/handle/20.500.12213/912
dc.description.abstractThe WWOX tumor suppressor is a WW domain-containing protein. Its function in the cell has been shown to be mediated, in part, by interacting with its partners through its firstWW(WW1) domain. Here, we demonstrated that WWOX viaWW1 domain interacts with p53 homolog, DNp63a. This protein–protein interaction stabilizes DNp63a, through antagonizing function of the E3 ubiquitin ligase ITCH, inhibits nuclear translocation of DNp63a into the nucleus and suppresses DNp63a transactivation function. Additionally, we found that this functional crosstalk reverses cancer cells resistance to cisplatin, mediated by DNp63a, and consequently renders these cells more sensitive to undergo apoptosis. These findings suggest a functional crosstalk between WWOX and DNp63a in tumorigenesis.en_US
dc.description.sponsorshipWe are grateful to all members of the Aqeilan’s lab for their technical help and fruitful discussion. This work was supported, in part, by funds from Israel Science Foundation (ISF; #12-0542) to RIA and Israeli Cancer Research Funds (ICRF) to RIA and ZS.en_US
dc.language.isoen_USen_US
dc.publisherSpringer Natureen_US
dc.titleTumor suppressor WWOX binds to DNp63a and sensitizes cancer cells to chemotherapyen_US
dc.typeArticleen_US


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