Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 최중섭 | - |
dc.date.accessioned | 2017-03-14T05:07:17Z | - |
dc.date.available | 2017-03-14T05:07:17Z | - |
dc.date.issued | 2015-07 | - |
dc.identifier.citation | MOLECULES AND CELLS, v. 38, NO 9, Page. 814-820 | en_US |
dc.identifier.issn | 1016-8478 | - |
dc.identifier.issn | 0219-1032 | - |
dc.identifier.uri | http://www.molcells.org/journal/view.html?doi=10.14348/molcells.2015.0144 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11754/26095 | - |
dc.description.abstract | PinX1, a nucleolar protein of 328 amino acids, inhibits telomerase activity, which leads to the shortening of telomeres. The C-terminal region of PinX1 is responsible for its nucleolar localization and binding with TERT, a catalytic component of telomerase. A fraction of TERT localizes to the nucleolus, but the role of TERT in the nucleolus is largely unknown. Here, we report a functional connection between PinX1 and TERT regarding PinX1 stability. The C-terminal of PinX1(20-328), a nucleolar fragment, was much more stable than the N-terminal of PinX1(1-204), a nuclear fragment. Interestingly, PinX1 was less stable in TERT-depleted cells and more stable in TERT-myc expressing cells. Stability assays for PinX1 truncation forms showed that both PinX1(1-328) and PinX1(205-328), nucleolar forms, were more rapidly degraded in TERT-depleted cells, while they were more stably maintained in TERT-overexpressing cells, compared to each of the controls. However, PinX(1-204) was degraded regardless of the TERT status. These results reveal that the stability of PinX1 is maintained in nucleolus in the presence of TERT and suggest a role of TERT in the regulation of PinX1 steady-state levels. | en_US |
dc.description.sponsorship | This work was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2010-0008254, 2014R 1A1A2054542 to BKO, 2013R1A1A2009090 to YHS), by the Ministry of Science, ICT & Future Planning (2011-0015638 to BKO), by Hanyang University (201200000002989 to JSC), and partly by Konkuk University's research support program for its faculty on sabbatical leave in 2013 to YHS. | en_US |
dc.language.iso | en | en_US |
dc.publisher | KOREAN SOC MOLECULAR & CELLULAR BIOLOGY | en_US |
dc.subject | nucleolus | en_US |
dc.subject | PinX1 | en_US |
dc.subject | protein stability | en_US |
dc.subject | TERT | en_US |
dc.title | Increased Stability of Nucleolar PinX1 in the Presence of TERT | en_US |
dc.type | Article | en_US |
dc.relation.no | 9 | - |
dc.relation.volume | 38 | - |
dc.identifier.doi | 10.14348/molcells.2015.0144 | - |
dc.relation.page | 814-820 | - |
dc.relation.journal | MOLECULES AND CELLS | - |
dc.contributor.googleauthor | Keo, Ponnarath | - |
dc.contributor.googleauthor | Choi, Joong Sub | - |
dc.contributor.googleauthor | Bae, Jaeman | - |
dc.contributor.googleauthor | Shim, Yhong-Hee | - |
dc.contributor.googleauthor | Oh, Bong-Kyeong | - |
dc.relation.code | 2015002733 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF MEDICINE[S] | - |
dc.sector.department | DEPARTMENT OF MEDICINE | - |
dc.identifier.pid | choiyjjy1 | - |
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