The lamin A/C Ig-fold undergoes cell density-dependent changes that alter epitope binding
Autor: | Melanie Wallace, Gregory R. Fedorchak, Richa Agrawal, Rachel M. Gilbert, Jineet Patel, Sangwoo Park, Matthew Paszek, Jan Lammerding |
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Jazyk: | angličtina |
Rok vydání: | 2023 |
Předmět: | |
Zdroj: | Nucleus, Vol 14, Iss 1 (2023) |
Druh dokumentu: | article |
ISSN: | 19491034 1949-1042 1949-1034 |
DOI: | 10.1080/19491034.2023.2180206 |
Popis: | ABSTRACTLamins A/C are nuclear intermediate filament proteins that are involved in diverse cellular mechanical and biochemical functions. Here, we report that recognition of Lamins A/C by a commonly used antibody (JOL-2) that binds the Lamin A/C Ig-fold and other antibodies targeting similar epitopes is highly dependent on cell density, even though Lamin A/Clevels do not change. We propose that the effect is caused by partial unfolding or masking of the C’E and/or EF loops of the Ig-fold in response to cell spreading. Surprisingly, JOL-2 antibody labeling was insensitive to disruption of cytoskeletal filaments or the Linker of Nucleoskeleton and Cytoskeleton (LINC) complex. Furthermore, neither nuclear stiffness nor nucleo-cytoskeletal force transmission changed with cell density. These findings are important for the interpretation of immunofluorescence data for Lamin A/C and also raise the intriguing prospect that the conformational changes may play a role in Lamin A/C mediated cellular function. |
Databáze: | Directory of Open Access Journals |
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