Nuclear myosin VI maintains replication fork stability
Jie Shi,
Kristine Hauschulte,
Ivan Mikicic,
Srijana Maharjan,
Valerie Arz,
Tina Strauch,
Jan B. Heidelberger,
Jonas V. Schaefer,
Birgit Dreier,
Andreas Plückthun,
Petra Beli,
Helle D. Ulrich () and
Hans-Peter Wollscheid ()
Additional contact information
Jie Shi: Institute of Molecular Biology gGmbH (IMB)
Kristine Hauschulte: Institute of Molecular Biology gGmbH (IMB)
Ivan Mikicic: Institute of Molecular Biology gGmbH (IMB)
Srijana Maharjan: Institute of Molecular Biology gGmbH (IMB)
Valerie Arz: Institute of Molecular Biology gGmbH (IMB)
Tina Strauch: Institute of Molecular Biology gGmbH (IMB)
Jan B. Heidelberger: Institute of Molecular Biology gGmbH (IMB)
Jonas V. Schaefer: Department of Biochemistry
Birgit Dreier: Department of Biochemistry
Andreas Plückthun: Department of Biochemistry
Petra Beli: Institute of Molecular Biology gGmbH (IMB)
Helle D. Ulrich: Institute of Molecular Biology gGmbH (IMB)
Hans-Peter Wollscheid: Institute of Molecular Biology gGmbH (IMB)
Nature Communications, 2023, vol. 14, issue 1, 1-13
Abstract:
Abstract The actin cytoskeleton is of fundamental importance for cellular structure and plasticity. However, abundance and function of filamentous actin in the nucleus are still controversial. Here we show that the actin-based molecular motor myosin VI contributes to the stabilization of stalled or reversed replication forks. In response to DNA replication stress, myosin VI associates with stalled replication intermediates and cooperates with the AAA ATPase Werner helicase interacting protein 1 (WRNIP1) in protecting these structures from DNA2-mediated nucleolytic attack. Using functionalized affinity probes to manipulate myosin VI levels in a compartment-specific manner, we provide evidence for the direct involvement of myosin VI in the nucleus and against a contribution of the abundant cytoplasmic pool during the replication stress response.
Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39517-y
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DOI: 10.1038/s41467-023-39517-y
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