Data and code for analyzing DSB mobility

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dc.contributor.author Richenhagen, Sebastian
dc.contributor.author Loewer, Alexander
dc.date.accessioned 2025-10-22T13:58:58Z
dc.date.created 2025-10-22
dc.date.issued 2025-10-22
dc.description Double-strand breaks (DSBs) are critical lesions in genomic DNA, and their accurate repair is essential for maintaining genome stability. The nuclear actin cytoskeleton has been implicated in homology-directed repair (HDR) of DSBs. However, the underlying mechanism remains poorly understood. Here, we report that Myosin VI (Myo6), an actin-based motor protein, cooperates with F-actin in end resection and DSB mobilization. Our findings reveal that Myo6 directly interacts with both KU70 and the ubiquitin-dependent segregase VCP to facilitate the extraction of the KU70/80 complex from chromatin. This process is supported by F-actin, revealing an interplay between nuclear actin dynamics and the DSB repair machinery. By elucidating the function of Myo6 and its direct interactions with key repair factors, our study provides mechanistic insight into how repair mechanisms rely on nuclear actin to safeguard genome integrity.
dc.identifier.uri https://tudatalib.ulb.tu-darmstadt.de/handle/tudatalib/4849
dc.identifier.uri https://doi.org/10.48328/tudatalib-1981
dc.rights.licenseCC-BY-4.0 (https://creativecommons.org/licenses/by/4.0)
dc.subject DSB mobility
dc.subject Myo6
dc.subject Actin
dc.subject.classification 2.11-03
dc.subject.ddc 570
dc.title Data and code for analyzing DSB mobility
dc.type Dataset
dc.type Software
dcterms.accessRights openAccess
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
tuda.agreements true
tuda.unit TUDa

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