4 results on '"Vasiliy O. Sysoev"'
Search Results
2. Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments
- Author
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Steven L. McKnight, Rong Hu, Vasiliy O. Sysoev, Lillian B. Sutherland, Masato Kato, and Dylan T. Murray
- Subjects
In situ ,intermediate filaments ,Protein Conformation ,Nuclear Magnetic Resonance ,Context (language use) ,Sequence (biology) ,Cell morphology ,Biochemistry ,Polymerization ,Low complexity ,Intermediate Filament Proteins ,Animals ,Intermediate filament ,Nuclear Magnetic Resonance, Biomolecular ,Multidisciplinary ,Chemistry ,Biological Sciences ,Order (biology) ,Domain (ring theory) ,Biophysics ,low-complexity proteins ,solid-state NMR ,cross-beta polymerization ,Drosophila ,Generic health relevance ,Biomolecular - Abstract
Significance The main point of our manuscript is focused on the structure of the low-complexity (LC) domain of the Tm1-I/C intermediate filament protein in the context of assembled intermediate filaments. We found that the LC tail domain of Tm1-I/C exists in precisely the same cross-β conformation within its proper biologic assembly as it does in labile, amyloid-like polymers made from the tail domain alone. This science represents a conceptually distinct advance that may form the cornerstone understanding of how the thousands of LC domains expressed in eukaryotic cells operate in a mechanistic sense, and stands in conflict with previous research claiming that LC domains function in the absence of molecular structure., The coiled-coil domains of intermediate filament (IF) proteins are flanked by regions of low sequence complexity. Whereas IF coiled-coil domains assume dimeric and tetrameric conformations on their own, maturation of eight tetramers into cylindrical IFs is dependent on either “head” or “tail” domains of low sequence complexity. Here we confirm that the tail domain required for assembly of Drosophila Tm1-I/C IFs functions by forming labile cross-β interactions. These interactions are seen in polymers made from the tail domain alone, as well as in assembled IFs formed by the intact Tm1-I/C protein. The ability to visualize such interactions in situ within the context of a discrete cellular assembly lends support to the concept that equivalent interactions may be used in organizing other dynamic aspects of cell morphology.
- Published
- 2020
3. An RNA-binding atypical tropomyosin recruits kinesin-1 dynamically to oskar mRNPs
- Author
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Anne Ephrussi, Artem Komissarov, Imre Gaspar, and Vasiliy O. Sysoev
- Subjects
0301 basic medicine ,RNA localization ,atypical tropomyosin isoform ,Dynein ,Kinesins ,RNA-binding protein ,macromolecular substances ,Tropomyosin ,Biology ,oskar ,General Biochemistry, Genetics and Molecular Biology ,Article ,Motor protein ,03 medical and health sciences ,Molecular motor ,Animals ,Drosophila Proteins ,active transport ,Membrane & Intracellular Transport ,Nuclear export signal ,oocyte ,Molecular Biology ,General Immunology and Microbiology ,urogenital system ,General Neuroscience ,Articles ,Molecular biology ,RNA binding protein ,Cell biology ,molecular motor ,Protein Transport ,030104 developmental biology ,Ribonucleoproteins ,Kinesin ,Drosophila ,Cell Adhesion, Polarity & Cytoskeleton ,Development & Differentiation ,Protein Binding - Abstract
Localization and local translation of oskar mRNA at the posterior pole of the Drosophila oocyte directs abdominal patterning and germline formation in the embryo. The process requires recruitment and precise regulation of motor proteins to form transport‐competent mRNPs. We show that the posterior‐targeting kinesin‐1 is loaded upon nuclear export of oskar mRNPs, prior to their dynein‐dependent transport from the nurse cells into the oocyte. We demonstrate that kinesin‐1 recruitment requires the DmTropomyosin1‐I/C isoform, an atypical RNA‐binding tropomyosin that binds directly to dimerizing oskar 3′UTRs. Finally, we show that a small but dynamically changing subset of oskar mRNPs gets loaded with inactive kinesin‐1 and that the motor is activated during mid‐oogenesis by the functionalized spliced oskar RNA localization element. This inefficient, dynamic recruitment of Khc decoupled from cargo‐dependent motor activation constitutes an optimized, coordinated mechanism of mRNP transport, by minimizing interference with other cargo‐transport processes and between the cargo‐associated dynein and kinesin‐1.
- Published
- 2016
4. An RNA-binding tropomyosin recruits kinesin-1 dynamically tooskarmRNPs
- Author
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Anne Ephrussi, Artem Komissarov, Imre Gaspar, and Vasiliy O. Sysoev
- Subjects
Genetics ,0303 health sciences ,Messenger RNA ,RNA localization ,urogenital system ,RNA ,macromolecular substances ,Biology ,Oocyte ,oskar ,Cell biology ,Motor protein ,03 medical and health sciences ,0302 clinical medicine ,medicine.anatomical_structure ,medicine ,Kinesin ,Nuclear export signal ,030217 neurology & neurosurgery ,030304 developmental biology - Abstract
Localization and local translation ofoskarmRNA at the posterior pole of theDrosophilaoocyte directs abdominal patterning and germline formation in the embryo. The process requires recruitment and precise regulation of motor proteins to form transport-competent mRNPs. We show that the posterior-targeting kinesin-1 is loaded upon nuclear export ofoskarmRNPs, prior to their dynein-dependent transport from the nurse cells into the oocyte. We demonstrate that kinesin-1 recruitment requires theDmTropomyosin1-I/C isoform, an atypical RNA-binding tropomyosin that binds directly to dimerizingoskar3’UTRs. Finally, we show that a small but dynamically changing subset ofoskarmRNPs gets loaded with inactive kinesin-1 and that the motor is activated during mid-oogenesis by the functionalized splicedoskarRNA localization element. This inefficient, dynamic recruitment of Khc decoupled from cargo-dependent motor activation constitutes an optmized, coordinated mechanism of mRNP transport, by minimizing interference with other cargo-transport processes and between the cargo associated dynein and kinesin-1.
- Published
- 2016
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