ID | 115930 |
Title Alternative | Pex14p phosphorylation regulates peroxisome import
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Author |
Yamashita, Koichiro
Kyushu University
Tamura, Shigehiko
Kyushu University
Honsho, Masanori
Kyushu University|Institute of Rheological Functions of Food
Yada, Hiroto
Kyushu University
Yagita, Yuichi
Kyushu University
Kosako, Hidetaka
Tokushima University
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Fujiki, Yukio
Kyushu University|Institute of Rheological Functions of Food
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Content Type |
Journal Article
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Description | Peroxisomal matrix proteins are imported into peroxisomes via membrane-bound docking/translocation machinery. One central component of this machinery is Pex14p, a peroxisomal membrane protein involved in the docking of Pex5p, the receptor for peroxisome targeting signal type 1 (PTS1). Studies in several yeast species have shown that Pex14p is phosphorylated in vivo, whereas no function has been assigned to Pex14p phosphorylation in yeast and mammalian cells. Here, we investigated peroxisomal protein import and its dynamics in mitotic mammalian cells. In mitotically arrested cells, Pex14p is phosphorylated at Ser-232, resulting in a lower import efficiency of catalase, but not the majority of proteins including canonical PTS1 proteins. Conformational change induced by the mitotic phosphorylation of Pex14p more likely increases homomeric interacting affinity and suppresses topological change of its N-terminal part, thereby giving rise to the retardation of Pex5p export in mitotic cells. Taken together, these data show that mitotic phosphorylation of Pex14p and consequent suppression of catalase import are a mechanism of protecting DNA upon nuclear envelope breakdown at mitosis.
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Journal Title |
Journal of Cell Biology
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ISSN | 00219525
15408140
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NCID | AA00694812
AA1203766X
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Publisher | Rockefeller University Press
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Volume | 219
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Issue | 10
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Start Page | e202001003
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Published Date | 2020-08-26
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Rights | This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
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language |
eng
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TextVersion |
Publisher
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departments |
Institute of Advanced Medical Sciences
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