Myosin VI in the nucleus of neurosecretory PC12 cells: Stimulation-dependent nuclear translocation and interaction with nuclear proteins*
Lukasz Majewski,Jolanta Nowak,Magdalena Sobczak,Olena Karatsai,Serhiy Havrylov,Robert Lenartowski,Małgorzata Suszek,Marta Lenartowska,Maria Jolanta Redowicz +8 more
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An increase in nuclear localization of MVI upon cell stimulation, and identification of potential nuclear localization (NLS) and nuclear export (NES) signals within MVI heavy chain are shown to be functional as the MVI nuclear presence was affected by the inhibitors of nuclear import and export.Abstract:
Myosin VI (MVI) is a unique actin-based motor protein moving towards the minus end of actin filaments, in the opposite direction than other known myosins. Besides well described functions of MVI in endocytosis and maintenance of Golgi apparatus, there are few reports showing its involvement in transcription. We previously demonstrated that in neurosecretory PC12 cells MVI was present in the cytoplasm and nucleus, and its depletion caused substantial inhibition of cell migration and proliferation. Here, we show an increase in nuclear localization of MVI upon cell stimulation, and identification of potential nuclear localization (NLS) and nuclear export (NES) signals within MVI heavy chain. These signals seem to be functional as the MVI nuclear presence was affected by the inhibitors of nuclear import (ivermectin) and export (leptomycin B). In nuclei of stimulated cells, MVI colocalized with active RNA polymerase II, BrUTP-containing transcription sites and transcription factor SP1 as well as SC35 and PML proteins, markers of nuclear speckles and PML bodies, respectively. Mass spectrometry analysis of samples of a GST-pull-down assay with the MVI tail domain as a "bait" identified several new potential MVI binding partners. Among them are proteins involved in transcription and post-transcriptional processes. We confirmed interaction of MVI with heterogeneous nuclear ribonucleoprotein U (hnRNPU) and nucleolin, proteins involved in pre-mRNA binding and transport, and nucleolar function, respectively. Our data provide an insight into mechanisms of involvement of MVI in nuclear processes via interaction with nuclear proteins and support a notion for important role(s) for MVI in gene expression.read more
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Long-Range Directional Movement of an Interphase Chromosome Site Dependent on Actin and Nuclear Myosin
TL;DR: The results suggest an active mechanism for fast and directed long-range interphase chromosome movements dependent directly or indirectly on actin/myosin.
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Mechanical Regulation of Transcription: Recent Advances.
Kaustubh Wagh,Kaustubh Wagh,Momoko Ishikawa,David A. Garcia,David A. Garcia,Diana A. Stavreva,Arpita Upadhyaya,Gordon L. Hager +7 more
TL;DR: In this paper, the authors highlight the importance of mechanotransduction as one of the governing principles of cancer progression and emphasize the need to conduct further studies of the molecular mechanisms involved in sensing mechanical cues and coordinating transcriptional responses.
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Myosin VI moves on nuclear actin filaments and supports long-range chromatin rearrangements
Andreas Große-Berkenbusch,Johannes Hettich,Timo Kuhn,Natalia Fili,Alexander W. Cook,Yukti Hari-Gupta,Palmer A,Streit L,Peter J.I. Ellis,Christopher P. Toseland,Gebhardt Jcm +10 more
TL;DR: Measurements reveal a transcription-coupled function of MVI in the nucleus, where it actively undergoes directed movement along nuclear actin filaments and is required for transcription-dependent long-range chromatin rearrangements.
Journal ArticleDOI
The LMTK-family of kinases: Emerging important players in cell physiology and pathogenesis.
Franz Wendler,Teodora-Maria Purice,Thomas Simon,Justin Stebbing,Justin Stebbing,Georgios Giamas +5 more
TL;DR: It is hypothesize that the primary role of LMTKs may dwell within the endocytic cargo recycling and/or nuclear receptor transport pathways, and expose them as potential valuable drug targets.
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Nuclear myosins – roles for molecular transporters and anchors
TL;DR: This Review will focus on the variation in structure of nuclear myosins, their nuclear import and their roles within transcription, DNA damage, chromatin organisation and viral infections, and discusses how the biochemical and biophysical properties of myosin lend themselves to nuclear processes.
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Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region
Nobuaki Kudo,Nobuaki Matsumori,Hiroshi Taoka,Daisuke Fujiwara,Erwin P. Schreiner,Barbara Wolff,Minoru Yoshida,Sueharu Horinouchi +7 more
TL;DR: Results show that the single cysteine residue determines LMB sensitivity and is selectively alkylated by LMB, leading to CRM1 inactivation.