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- Publisher
- Springer Journals
- Copyright
- Copyright © 2010 by Springer Basel AG
- Subject
- Life Sciences; Biomedicine general; Cell Biology; Life Sciences, general ; Biochemistry, general
- ISSN
- 1420-682X
- eISSN
- 1420-9071
- DOI
- 10.1007/s00018-010-0535-z
- pmid
- 20922455
- Publisher site
- See Article on Publisher Site
Abstract
Cell polarization is a fundamental process underpinning organismal development, and tissue homeostasis, which requires an orchestrated interplay of nuclear, cytoskeletal, and centrosomal structures. The underlying molecular mechanisms, however, still remain elusive. Here we report that kinesin-1/nesprin-2/SUN-domain macromolecular assemblies, spanning the entire nuclear envelope (NE), function in cell polarization by anchoring cytoskeletal structures to the nuclear lamina. Nesprin-2 forms complexes with the kinesin-1 motor protein apparatus by associating with and recruiting kinesin light chain1 (KLC1) to the outer nuclear membrane. Similar to nesprin-2, KLC1 requires lamin A/C for proper NE localization. The depletion of nesprin-2 or KLC1, or the uncoupling of nesprin-2/SUN-domain protein associations impairs cell polarization during wounding and dislodges the centrosome from the NE. In addition nesprin-2 loss has profound effects on KLC1 levels, the cytoskeleton, and Golgi apparatus organization. Collectively these data show that NE-associated proteins are pivotal determinants of cell architecture and polarization.
Journal
Cellular and Molecular Life Sciences – Springer Journals
Published: Oct 5, 2010