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Role of the nuclear membrane protein Emerin in front-rear polarity of the nucleus
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Role of the nuclear membrane protein Emerin in front-rear polarity of the nucleus
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Role of the nuclear membrane protein Emerin in front-rear polarity of the nucleus
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Journal Article
Role of the nuclear membrane protein Emerin in front-rear polarity of the nucleus
2020
Overview
Cell polarity refers to the intrinsic asymmetry of cells, including the orientation of the cytoskeleton. It affects cell shape and structure as well as the distribution of proteins and organelles. In migratory cells, front-rear polarity is essential and dictates movement direction. While the link between the cytoskeleton and nucleus is well-studied, we aim to investigate if front-rear polarity can be transmitted to the nucleus. We show that the knock-down of emerin, an integral protein of the nuclear envelope, abolishes preferential localization of several nuclear proteins. We propose that the frontally biased localization of the endoplasmic reticulum, through which emerin reaches the nuclear envelope, is sufficient to generate its observed bias. In primary emerin-deficient myoblasts, its expression partially rescues the polarity of the nucleus. Our results demonstrate that front-rear cell polarity is transmitted to the nucleus and that emerin is an important determinant of nuclear polarity.
During cell migration, cells are polarized with distinct front vs. rear regions but whether and how polarity is transmitted to the nucleus is unclear. Here the authors show that frontally-biased endoplasmic reticulum and the nuclear membrane protein Emerin contribute to front-rear nuclear cell polarity.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/106
/ 13/109
/ 13/89
/ 14
/ 14/19
/ 14/28
/ 14/32
/ 14/35
/ 14/63
/ Cell Nucleus - ultrastructure
/ Fluorescent Antibody Technique
/ Humanities and Social Sciences
/ Humans
/ Membrane Proteins - metabolism
/ Microscopy, Electron, Transmission
/ Nuclear Envelope - metabolism
/ Nuclear Envelope - ultrastructure
/ Nuclear Proteins - metabolism
/ Polarity
/ Proteins
/ Science
