N-terminal tags impair the ability of lamin A to provide structural support to the nucleus

Author:

Odell Jacob12ORCID,Lammerding Jan13ORCID

Affiliation:

1. Weill Institute for Cell and Molecular Biology, Cornell University 1 , Ithaca, NY 14853 , USA

2. Cornell University 2 Graduate Field of Biochemistry, Molecular and Cell Biology , , Ithaca, NY 14853 , USA

3. Meinig School of Biomedical Engineering, Cornell University 3 , Ithaca, NY 14853 , USA

Abstract

ABSTRACT Lamins are intermediate filament proteins that contribute to numerous cellular functions, including nuclear morphology and mechanical stability. The N-terminal head domain of lamin is crucial for higher order filament assembly and function, yet the effects of commonly used N-terminal tags on lamin function remain largely unexplored. Here, we systematically studied the effect of two differently sized tags on lamin A (LaA) function in a mammalian cell model engineered to allow for precise control of expression of tagged lamin proteins. Untagged, FLAG-tagged and GFP-tagged LaA completely rescued nuclear shape defects when expressed at similar levels in lamin A/C-deficient (Lmna–/–) MEFs, and all LaA constructs prevented increased nuclear envelope ruptures in these cells. N-terminal tags, however, altered the nuclear localization of LaA and impaired the ability of LaA to restore nuclear deformability and to recruit emerin to the nuclear membrane in Lmna–/– MEFs. Our finding that tags impede some LaA functions but not others might explain the partial loss of function phenotypes when tagged lamins are expressed in model organisms and should caution researchers using tagged lamins to study the nucleus.

Funder

Volkswagen Foundation

National Institutes of Health

National Science Foundation

Publisher

The Company of Biologists

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1. First person – Jacob Odell;Journal of Cell Science;2024-08-15

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