ZMPSTE24 missense mutations that cause progeroid diseases decrease prelamin A cleavage activity and/or protein stability

Autor: Eric D. Spear, Erh-Ting Hsu, Laiyin Nie, Elisabeth P. Carpenter, Christine A. Hrycyna, Susan Michaelis

Publikováno v: Disease Models & Mechanisms, Vol 11, Iss 7 (2018)

The human zinc metalloprotease ZMPSTE24 is an integral membrane protein crucial for the final step in the biogenesis of the nuclear scaffold protein lamin A, encoded by LMNA. After farnesylation and carboxyl methylation of its C-terminal CAAX motif,

Externí odkaz: https://doaj.org/article/6c0979a4e97a4be383f99598cba015bf

a-Factor Analogues Containing Alkyne- and Azide-Functionalized Isoprenoids Are Efficiently Enzymatically Processed and Retain Wild-Type Bioactivity

Autor: Erh-Ting Hsu, Elena E. Ganusova, Jeffrey M. Becker, Elena R. Werst, Veronica Diaz-Rodriguez, Mark D. Distefano, Christine A. Hrycyna

Publikováno v: Bioconjugate Chemistry

Protein prenylation is a post-translational modification that involves the addition of one or two isoprenoid groups to the C-terminus of selected proteins using either farnesyl diphosphate or geranylgeranyl diphosphate. Three crucial enzymatic steps

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51036baa9bb286545fc3cf2339d60c6d
https://doi.org/10.1021/acs.bioconjchem.7b00648

A Quantitative FRET Assay for the Upstream Cleavage Activity of the Integral Membrane Proteases Human ZMPSTE24 and Yeast Ste24

Autor: Jeffrey S. Vervacke, Erh-Ting Hsu, Christine A. Hrycyna, Mark D. Distefano

Publikováno v: Methods in Molecular Biology ISBN: 9781493995318

The integral membrane protease ZMPSTE24 plays an important role in the lamin A maturation pathway. ZMPSTE24 is the only known enzyme to cleave the last 15 residues from the C-terminus of prelamin A, including a farnesylated and carboxyl methylated cy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5cb31eaf66bbcaf0d7330ee04ab55f8d
https://doi.org/10.1007/978-1-4939-9532-5_21

ZMPSTE24 missense mutations that cause progeroid diseases decrease prelamin A cleavage activity and/or protein stability

Autor: Christine A. Hrycyna, Eric D. Spear, Laiyin Nie, Susan Michaelis, Erh-Ting Hsu, Elisabeth P. Carpenter

Publikováno v: Disease Models & Mechanisms, Vol 11, Iss 7 (2018)
Disease Models & Mechanisms

The human zinc metalloprotease ZMPSTE24 is an integral membrane protein crucial for the final step in the biogenesis of the nuclear scaffold protein lamin A, encoded by LMNA. After farnesylation and carboxyl methylation of its C-terminal CAAX motif,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62a8284035f241daa6e40fa05b193984
http://dmm.biologists.org/content/11/7/dmm033670

AIM2 inflammasome is activated by pharmacological disruption of nuclear envelope integrity

Autor: Bojan Bujisic, Léa Zaffalon, Manfredo Quadroni, Gianluca Frera, Fabio Martinon, Aubry Tardivel, Aude De Gassart, Jérôme Lugrin, Yvan Jamilloux, Stefanie Siegert, Thomas Henry, Petr Broz, Erh-Ting Hsu, Antonia Di Micco, Christine A. Hrycyna

Publikováno v: Proceedings of the National Acadamy of Science
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2016, 113 (32), pp.E4671-4680. ⟨10.1073/pnas.1602419113⟩
Proceedings of the National Academy of Sciences of the United States of America, 2016, 113 (32), pp.E4671-4680. ⟨10.1073/pnas.1602419113⟩
Europe PubMed Central
Proceedings of the National Academy of Sciences of the United States of America, vol. 113, no. 32, pp. E4671-80

International audience; Inflammasomes are critical sensors that convey cellular stress and pathogen presence to the immune system by activating inflammatory caspases and cytokines such as IL-1β. The nature of endogenous stress signals that activate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b35901cf03bca6b3853b64a97571678d
https://www.ncbi.nlm.nih.gov/pubmed/27462105