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Mitofusin 1 is degraded at G2/M phase through ubiquitylation by MARCH5

DC Field Value Language
dc.contributor.authorPark, YY-
dc.contributor.authorCho, H-
dc.date.accessioned2013-04-23-
dc.date.available2013-04-23-
dc.date.issued2012-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/7825-
dc.description.abstractBACKGROUND: Mitochondria exhibit a dynamic morphology in cells and their biogenesis and function are integrated with the nuclear cell cycle. In mitotic cells, the filamentous network structure of mitochondria takes on a fragmented form. To date, however, whether mitochondrial fusion activity is regulated in mitosis has yet to be elucidated.



FINDINGS: Here, we report that mitochondria were found to be fragmented in G2 phase prior to mitotic entry. Mitofusin 1 (Mfn1), a mitochondrial fusion protein, interacted with cyclin B1, and their interactions became stronger in G2/M phase. In addition, MARCH5, a mitochondrial E3 ubiquitin ligase, reduced Mfn1 levels and the MARCH5-mediated Mfn1 ubiquitylation were enhanced in G2/M phase.



CONCLUSIONS: Mfn1 is degraded through the MARCH5-mediated ubiquitylation in G2/M phase and the cell cycle-dependent degradation of Mfn1 could be facilitated by interaction with cyclin B1/Cdk1 complexes.
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dc.language.isoen-
dc.titleMitofusin 1 is degraded at G2/M phase through ubiquitylation by MARCH5-
dc.typeArticle-
dc.identifier.pmid23253261-
dc.identifier.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3542011/-
dc.contributor.affiliatedAuthor박, 용예-
dc.contributor.affiliatedAuthor조, 혜성-
dc.type.localJournal Papers-
dc.identifier.doi10.1186/1747-1028-7-25-
dc.citation.titleCell division-
dc.citation.volume7-
dc.citation.number1-
dc.citation.date2012-
dc.citation.startPage25-
dc.citation.endPage25-
dc.identifier.bibliographicCitationCell division, 7(1):25-25, 2012-
dc.identifier.eissn1747-1028-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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