Selective inhibitors of SIRT2 regulate perinuclear α-tubulin acetylation, migration, and invasion of breast cancer cells

Research output: Contribution to journal › Journal article › Research

Standard

Selective inhibitors of SIRT2 regulate perinuclear α-tubulin acetylation, migration, and invasion of breast cancer cells. / Nielsen, Alexander L; Rajabi, Nima; Kudo, Norio; Larsen, Kathrine Lundø; Fontenas, Martin; Lucidi, Alessia; Madsen, Andreas S; Yoshida, Minoru; Olsen, Christian Adam.

In: bioRxiv, 2020.

Research output: Contribution to journal › Journal article › Research

Harvard

Nielsen, AL, Rajabi, N, Kudo, N, Larsen, KL, Fontenas, M, Lucidi, A, Madsen, AS, Yoshida, M & Olsen, CA 2020, 'Selective inhibitors of SIRT2 regulate perinuclear α-tubulin acetylation, migration, and invasion of breast cancer cells', bioRxiv. https://doi.org/10.1101/2020.03.20.000380

APA

Nielsen, A. L., Rajabi, N., Kudo, N., Larsen, K. L., Fontenas, M., Lucidi, A., Madsen, A. S., Yoshida, M., & Olsen, C. A. (2020). Selective inhibitors of SIRT2 regulate perinuclear α-tubulin acetylation, migration, and invasion of breast cancer cells. bioRxiv. https://doi.org/10.1101/2020.03.20.000380

Vancouver

Nielsen AL, Rajabi N, Kudo N, Larsen KL, Fontenas M, Lucidi A et al. Selective inhibitors of SIRT2 regulate perinuclear α-tubulin acetylation, migration, and invasion of breast cancer cells. bioRxiv. 2020. https://doi.org/10.1101/2020.03.20.000380

Author

Nielsen, Alexander L ; Rajabi, Nima ; Kudo, Norio ; Larsen, Kathrine Lundø ; Fontenas, Martin ; Lucidi, Alessia ; Madsen, Andreas S ; Yoshida, Minoru ; Olsen, Christian Adam. / Selective inhibitors of SIRT2 regulate perinuclear α-tubulin acetylation, migration, and invasion of breast cancer cells. In: bioRxiv. 2020.

Bibtex

@article{fff424de32c94b5b945666f414e89871,
title = "Selective inhibitors of SIRT2 regulate perinuclear α-tubulin acetylation, migration, and invasion of breast cancer cells",
abstract = "Sirtuin 2 (SIRT2) is a protein deacylase enzyme that has been reported to remove both acetyl groups and longer chain acyl groups from lysine residues in post-translationally modified proteins. It affects diverse biological functions in the cell and has been considered a drug target in relation to both neurodegenerative diseases and cancer. Therefore, access to good chemical tool compounds are essential for the continued investigation of the complex function of this enzyme. Here, we report a collection of probes that are potent, selective, stable in serum, water soluble, amenable to cell culture experiments, and inhibit both SIRT2 deacetylation and demyristoylation. Compared to the current landscape of SIRT2 inhibitors, this is a unique ensemble of features built into a single compound. We expect the developed chemotypes to find broad applications in the interrogation of SIRT2 functions in both healthy and diseased cells to provide a foundation for the development of new therapeutics in the future.",
author = "Nielsen, {Alexander L} and Nima Rajabi and Norio Kudo and Larsen, {Kathrine Lund{\o}} and Martin Fontenas and Alessia Lucidi and Madsen, {Andreas S} and Minoru Yoshida and Olsen, {Christian Adam}",
year = "2020",
doi = "10.1101/2020.03.20.000380",
language = "Dansk",
journal = "bioRxiv",
publisher = "Cold Spring Harbor Laboratory",

}

RIS

TY - JOUR

T1 - Selective inhibitors of SIRT2 regulate perinuclear α-tubulin acetylation, migration, and invasion of breast cancer cells

AU - Nielsen, Alexander L

AU - Rajabi, Nima

AU - Kudo, Norio

AU - Larsen, Kathrine Lundø

AU - Fontenas, Martin

AU - Lucidi, Alessia

AU - Madsen, Andreas S

AU - Yoshida, Minoru

AU - Olsen, Christian Adam

PY - 2020

Y1 - 2020

N2 - Sirtuin 2 (SIRT2) is a protein deacylase enzyme that has been reported to remove both acetyl groups and longer chain acyl groups from lysine residues in post-translationally modified proteins. It affects diverse biological functions in the cell and has been considered a drug target in relation to both neurodegenerative diseases and cancer. Therefore, access to good chemical tool compounds are essential for the continued investigation of the complex function of this enzyme. Here, we report a collection of probes that are potent, selective, stable in serum, water soluble, amenable to cell culture experiments, and inhibit both SIRT2 deacetylation and demyristoylation. Compared to the current landscape of SIRT2 inhibitors, this is a unique ensemble of features built into a single compound. We expect the developed chemotypes to find broad applications in the interrogation of SIRT2 functions in both healthy and diseased cells to provide a foundation for the development of new therapeutics in the future.

AB - Sirtuin 2 (SIRT2) is a protein deacylase enzyme that has been reported to remove both acetyl groups and longer chain acyl groups from lysine residues in post-translationally modified proteins. It affects diverse biological functions in the cell and has been considered a drug target in relation to both neurodegenerative diseases and cancer. Therefore, access to good chemical tool compounds are essential for the continued investigation of the complex function of this enzyme. Here, we report a collection of probes that are potent, selective, stable in serum, water soluble, amenable to cell culture experiments, and inhibit both SIRT2 deacetylation and demyristoylation. Compared to the current landscape of SIRT2 inhibitors, this is a unique ensemble of features built into a single compound. We expect the developed chemotypes to find broad applications in the interrogation of SIRT2 functions in both healthy and diseased cells to provide a foundation for the development of new therapeutics in the future.

U2 - 10.1101/2020.03.20.000380

DO - 10.1101/2020.03.20.000380

M3 - Tidsskriftartikel

JO - bioRxiv

JF - bioRxiv

ER -

ID: 239223486