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Journal Article

Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane.

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Lenz,  C.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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3164694_Suppl.pdf
(Supplementary material), 19MB

Citation

James, C., Müller, M., Goldberg, M. W., Lenz, C., Urlaub, H., & Kehlenbach, R. H. (2019). Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane. The Journal of Biological Chemistry, 294(44), 16241-16254. doi:10.1074/jbc.RA118.007283.


Cite as: https://hdl.handle.net/21.11116/0000-0004-AF80-6
Abstract
VAPB (vesicle-associated membrane protein-associated protein B) is a tail-anchored protein that is present at several contact sites of the endoplasmic reticulum (ER). We now show by immunoelectron microscopy that VAPB also localizes to the inner nuclear membrane (INM). Using a modified APEX2 (enhanced ascorbate peroxidase 2)-approach with rapamycin-dependent targeting of the peroxidase to a protein of interest, we searched for proteins that are in close proximity to VAPB, particularly at the INM. In combination with stable isotope labeling with amino acids in cell culture (SILAC), we confirmed many well-known interaction partners at the level of the ER with a clear distinction between specific and non-specific hits. Furthermore, we identified emerin, TMEM43 and ELYS as potential interaction partners of VAPB at the INM and the nuclear pore complex, respectively.