2012
DOI: 10.1016/j.bbrc.2012.05.139
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Cytoplasmic sequestration of the tumor suppressor p53 by a heat shock protein 70 family member, mortalin, in human colorectal adenocarcinoma cell lines

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Cited by 42 publications
(30 citation statements)
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“…This expression may be related to testosterone related testicular damage; as p53 can be highly expressed in testes under cellular stress as its intracellular concentration increase to a level that can be detected [46,47].…”
Section: Discussionmentioning
confidence: 99%
“…This expression may be related to testosterone related testicular damage; as p53 can be highly expressed in testes under cellular stress as its intracellular concentration increase to a level that can be detected [46,47].…”
Section: Discussionmentioning
confidence: 99%
“…Cytoplasmic accumulation and retention of p53 has also been found in about 40% of breast cancer tissues, retinoblastomas, glioblastomas, and hepatocellular carcinomas [41, 52]. The retention of cytoplasmic p53 by the heat shock protein Mortalin has been reported for several tumor cell types, including human glioblastomas, hepatocellular carcinomas, and colorectal adenocarcinomas [53]. In contrast to the retention of wild-type p53 in the cytoplasm, mutant p53 tends to accumulate in the nucleus of colorectal adenocarcinoma [54].…”
Section: Mislocalization Of Tumor Suppressor Proteinsmentioning
confidence: 99%
“…This current study suggests UBXN2A binds to mortalin's protein binding pocket and interferes with mortalin's binding partners (Dundas et al 2005;Gestl and Anne Bottger 2012;Guo et al 2014;Sadekova et al 1997) resulting in inactivation of mortalin oncoprotein in cancer cells. Part of the apoptotic resistance of cancer cells is mediated by activation of WT-mortalin in cancer cells, including osteosarcoma (Wadhwa et al 2015).…”
Section: Discussionmentioning
confidence: 99%
“…We hypothesized that UBXN2A binding to mortalin's binding pocket can also disrupt mortalin's interaction with partners, antagonize oncogenic function of mortalin, and eventually induce cell cytotoxicity in cancer cells. Overexpression of mortalin correlates with a higher proliferation rate, colony forming efficacy, motility, and tumor forming capacity; poor survival; and increased resistance to therapies (Dundas et al 2005;Gestl and Anne Bottger 2012;Guo et al 2014;Sadekova et al 1997). …”
Section: Ubxn2a Interferes With Cell Proliferation and Migration Of Cmentioning
confidence: 99%