A masked initiation region in retinoblastoma protein regulates its proteasomal degradation
Human papilloma virus (HPV) E7 protein destabilizes the retinoblastoma protein (Rb) by inducing its ubiquitination in cervical cancer cells, however proteasomal degradation requires cleavage of Rb after Lys 810 and so far it has been unclear how Rb cleavage contributes to its degradation. Here, the...
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Nature Portfolio
2020
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oai:doaj.org-article:efa1fd80046b433d9c08b09e1c821f0f2021-12-02T17:32:12ZA masked initiation region in retinoblastoma protein regulates its proteasomal degradation10.1038/s41467-020-16003-32041-1723https://doaj.org/article/efa1fd80046b433d9c08b09e1c821f0f2020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16003-3https://doaj.org/toc/2041-1723Human papilloma virus (HPV) E7 protein destabilizes the retinoblastoma protein (Rb) by inducing its ubiquitination in cervical cancer cells, however proteasomal degradation requires cleavage of Rb after Lys 810 and so far it has been unclear how Rb cleavage contributes to its degradation. Here, the authors combine cell based and in vitro assays and show that calpain cleavage exposes a region in Rb that is recognized by the proteasome, leading to rapid proteolysis of Rb, whereas the proteasome cannot initiate degradation efficiently on full-length Rb.Takuya TomitaJon M. HuibregtseAndreas MatouschekNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-8 (2020) |
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Science Q Takuya Tomita Jon M. Huibregtse Andreas Matouschek A masked initiation region in retinoblastoma protein regulates its proteasomal degradation |
description |
Human papilloma virus (HPV) E7 protein destabilizes the retinoblastoma protein (Rb) by inducing its ubiquitination in cervical cancer cells, however proteasomal degradation requires cleavage of Rb after Lys 810 and so far it has been unclear how Rb cleavage contributes to its degradation. Here, the authors combine cell based and in vitro assays and show that calpain cleavage exposes a region in Rb that is recognized by the proteasome, leading to rapid proteolysis of Rb, whereas the proteasome cannot initiate degradation efficiently on full-length Rb. |
format |
article |
author |
Takuya Tomita Jon M. Huibregtse Andreas Matouschek |
author_facet |
Takuya Tomita Jon M. Huibregtse Andreas Matouschek |
author_sort |
Takuya Tomita |
title |
A masked initiation region in retinoblastoma protein regulates its proteasomal degradation |
title_short |
A masked initiation region in retinoblastoma protein regulates its proteasomal degradation |
title_full |
A masked initiation region in retinoblastoma protein regulates its proteasomal degradation |
title_fullStr |
A masked initiation region in retinoblastoma protein regulates its proteasomal degradation |
title_full_unstemmed |
A masked initiation region in retinoblastoma protein regulates its proteasomal degradation |
title_sort |
masked initiation region in retinoblastoma protein regulates its proteasomal degradation |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/efa1fd80046b433d9c08b09e1c821f0f |
work_keys_str_mv |
AT takuyatomita amaskedinitiationregioninretinoblastomaproteinregulatesitsproteasomaldegradation AT jonmhuibregtse amaskedinitiationregioninretinoblastomaproteinregulatesitsproteasomaldegradation AT andreasmatouschek amaskedinitiationregioninretinoblastomaproteinregulatesitsproteasomaldegradation AT takuyatomita maskedinitiationregioninretinoblastomaproteinregulatesitsproteasomaldegradation AT jonmhuibregtse maskedinitiationregioninretinoblastomaproteinregulatesitsproteasomaldegradation AT andreasmatouschek maskedinitiationregioninretinoblastomaproteinregulatesitsproteasomaldegradation |
_version_ |
1718380406169927680 |