Ubiquitin C-terminal hydrolase isozyme L1 is associated with shelterin complex at interstitial telomeric sites

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dc.contributor.authorIlic, Aleksandar
dc.contributor.authorLu, Sumin
dc.contributor.authorBhatia, Vikram
dc.contributor.authorBegum, Farhana
dc.contributor.authorKlonisch, Thomas
dc.contributor.authorAgarwal, Prasoon
dc.contributor.authorXu, Wayne
dc.contributor.authorDavie, James R
dc.date.accessioned2017-12-04T16:26:28Z
dc.date.available2017-12-04T16:26:28Z
dc.date.issued2017-11-10
dc.date.updated2017-12-01T04:54:50Z
dc.description.abstractAbstract Background Ubiquitin C-terminal hydrolase isozyme L1 (UCHL1) is primarily expressed in neuronal cells and neuroendocrine cells and has been associated with various diseases, including many cancers. It is a multifunctional protein involved in deubiquitination, ubiquitination and ubiquitin homeostasis, but its specific roles are disputed and still generally undetermined. Results Herein, we demonstrate that UCHL1 is associated with genomic DNA in certain prostate cancer cell lines, including DU 145 cells derived from a brain metastatic site, and in HEK293T embryonic kidney cells with a neuronal lineage. Chromatin immunoprecipitation and sequencing revealed that UCHL1 localizes to TTAGGG repeats at telomeres and interstitial telomeric sequences, as do TRF1 and TRF2, components of the shelterin complex. A weak or transient interaction between UCHL1 and the shelterin complex was confirmed by immunoprecipitation and proximity ligation assays. UCHL1 and RAP1, also known as TERF2IP and a component of the shelterin complex, were bound to the nuclear scaffold. Conclusions We demonstrated a novel feature of UCHL1 in binding telomeres and interstitial telomeric sites.
dc.identifier.citationEpigenetics & Chromatin. 2017 Nov 10;10(1):54
dc.identifier.urihttp://dx.doi.org/10.1186/s13072-017-0160-2
dc.identifier.urihttp://hdl.handle.net/1993/32708
dc.language.rfc3066en
dc.rightsopen accessen_US
dc.rights.holderThe Author(s)
dc.titleUbiquitin C-terminal hydrolase isozyme L1 is associated with shelterin complex at interstitial telomeric sites
dc.typeJournal Article
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