國家衛生研究院 NHRI:Item 3990099045/2181
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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/2181


    Title: Apoptotic cleavage of NuMA at the C-terminal end is related to nuclear disruption and death amplification
    Authors: Lin, HH;Hsu, HL;Yeh, NH
    Contributors: Division of Molecular and Genomic Medicine
    Abstract: NuMA is a nuclear matrix protein in interphase and distributes to the spindle poles during mitosis. While the essential function of NuMA for mitotic spindle assembly is well established, a structural role of NuMA in interphase nucleus has also been proposed. Several observations suggest that the apoptotic degradation of NuMA may relate to chromatin condensation and micronucleation. Here we demonstrate that four apoptotic cleavage sites are clustered at a junction between the globular tail and the central coiled-coil domains of NuMA. Cleavage of a caspase-6-sensitive site at D-1705 produced the R-form, a major tail-less product of NuMA during apoptosis. The other two cleavage sites were defined at D-1726 and D-1747 that were catalyzed, respectively, by caspase-3 and an unknown aspartase. A NuMA deletion mutant missing the entire cleavage region of residues 1701-1828 resisted degradation and protected cells from nuclear disruption upon apoptotic attack. Under such conditions, cytochrome c was released from mitochondria, but the subsequent apoptotic events such as caspase-3 activation, poly(ADP-ribose) polymerase degradation, and DNA fragmentation were attenuated. Conversely, the tail-less NuMA alone, a mutant mimicking the R-form, induced chromatin condensation and activated the death machinery. It supports that intact NuMA is a structural element in maintaining nuclear integrity.
    Keywords: Medicine, Research & Experimental
    Date: 2007-09
    Relation: Journal of Biomedical Science. 2007 Sep;14(5):681-694.
    Link to: http://dx.doi.org/10.1007/s11373-007-9165-3
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=1021-7770&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000249446300012
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=34548661070
    Appears in Collections:[Hsin-Ling Hsu] Periodical Articles

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