Nuclear lamins: Structure and function in mechanobiology
Nuclear lamins are type V intermediate filament proteins that polymerize into complex filamentous meshworks at the nuclear periphery and in less structured forms throughout the nucleoplasm. Lamins interact with a wide range of nuclear proteins and are involved in numerous nuclear and cellular functi...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
AIP Publishing LLC
2022-03-01
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| Series: | APL Bioengineering |
| Online Access: | http://dx.doi.org/10.1063/5.0082656 |
| _version_ | 1819047399001161728 |
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| author | Amir Vahabikashi Stephen A. Adam Ohad Medalia Robert D. Goldman |
| author_facet | Amir Vahabikashi Stephen A. Adam Ohad Medalia Robert D. Goldman |
| author_sort | Amir Vahabikashi |
| collection | DOAJ |
| description | Nuclear lamins are type V intermediate filament proteins that polymerize into complex filamentous meshworks at the nuclear periphery and in less structured forms throughout the nucleoplasm. Lamins interact with a wide range of nuclear proteins and are involved in numerous nuclear and cellular functions. Within the nucleus, they play roles in chromatin organization and gene regulation, nuclear shape, size, and mechanics, and the organization and anchorage of nuclear pore complexes. At the whole cell level, they are involved in the organization of the cytoskeleton, cell motility, and mechanotransduction. The expression of different lamin isoforms has been associated with developmental progression, differentiation, and tissue-specific functions. Mutations in lamins and their binding proteins result in over 15 distinct human diseases, referred to as laminopathies. The laminopathies include muscular (e.g., Emery–Dreifuss muscular dystrophy and dilated cardiomyopathy), neurological (e.g., microcephaly), and metabolic (e.g., familial partial lipodystrophy) disorders as well as premature aging diseases (e.g., Hutchinson–Gilford Progeria and Werner syndromes). How lamins contribute to the etiology of laminopathies is still unknown. In this review article, we summarize major recent findings on the structure, organization, and multiple functions of lamins in nuclear and more global cellular processes. |
| first_indexed | 2024-12-21T10:59:44Z |
| format | Article |
| id | doaj.art-11845f71dba34e3d8071d5a8b75a421e |
| institution | Directory Open Access Journal |
| issn | 2473-2877 |
| language | English |
| last_indexed | 2024-12-21T10:59:44Z |
| publishDate | 2022-03-01 |
| publisher | AIP Publishing LLC |
| record_format | Article |
| series | APL Bioengineering |
| spelling | doaj.art-11845f71dba34e3d8071d5a8b75a421e2022-12-21T19:06:22ZengAIP Publishing LLCAPL Bioengineering2473-28772022-03-0161011503011503-1110.1063/5.0082656Nuclear lamins: Structure and function in mechanobiologyAmir Vahabikashi0Stephen A. Adam1Ohad Medalia2Robert D. Goldman3 Department of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA Department of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA Department of Biochemistry, University of Zurich, Zurich, Switzerland Department of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USANuclear lamins are type V intermediate filament proteins that polymerize into complex filamentous meshworks at the nuclear periphery and in less structured forms throughout the nucleoplasm. Lamins interact with a wide range of nuclear proteins and are involved in numerous nuclear and cellular functions. Within the nucleus, they play roles in chromatin organization and gene regulation, nuclear shape, size, and mechanics, and the organization and anchorage of nuclear pore complexes. At the whole cell level, they are involved in the organization of the cytoskeleton, cell motility, and mechanotransduction. The expression of different lamin isoforms has been associated with developmental progression, differentiation, and tissue-specific functions. Mutations in lamins and their binding proteins result in over 15 distinct human diseases, referred to as laminopathies. The laminopathies include muscular (e.g., Emery–Dreifuss muscular dystrophy and dilated cardiomyopathy), neurological (e.g., microcephaly), and metabolic (e.g., familial partial lipodystrophy) disorders as well as premature aging diseases (e.g., Hutchinson–Gilford Progeria and Werner syndromes). How lamins contribute to the etiology of laminopathies is still unknown. In this review article, we summarize major recent findings on the structure, organization, and multiple functions of lamins in nuclear and more global cellular processes.http://dx.doi.org/10.1063/5.0082656 |
| spellingShingle | Amir Vahabikashi Stephen A. Adam Ohad Medalia Robert D. Goldman Nuclear lamins: Structure and function in mechanobiology APL Bioengineering |
| title | Nuclear lamins: Structure and function in mechanobiology |
| title_full | Nuclear lamins: Structure and function in mechanobiology |
| title_fullStr | Nuclear lamins: Structure and function in mechanobiology |
| title_full_unstemmed | Nuclear lamins: Structure and function in mechanobiology |
| title_short | Nuclear lamins: Structure and function in mechanobiology |
| title_sort | nuclear lamins structure and function in mechanobiology |
| url | http://dx.doi.org/10.1063/5.0082656 |
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