Kinetics of the thapsigargin-induced Ca2+ mobilisation: A quantitative analysis in the HEK-293 cell line

Autor: Tillman Pick, Igor Gamayun, René Tinschert, Adolfo Cavalié

Publikováno v: Frontiers in Physiology, Vol 14 (2023)

Thapsigargin (TG) inhibits the sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) pump and, when applied acutely, it initiates a Ca2+ mobilisation that begins with the loss of Ca2+ from the endoplasmic reticulum (ER) and culminates with store-operated C

Externí odkaz: https://doaj.org/article/af397b99b97b4ce1aadbc47f5bb27b34

Antagonizing Sec62 function in intracellular Ca2+ homeostasis represents a novel therapeutic strategy for head and neck cancer

Autor: Sandrina Körner, Tillman Pick, Florian Bochen, Silke Wemmert, Christina Körbel, Michael D. Menger, Adolfo Cavalié, Jan-Philipp Kühn, Bernhard Schick, Maximilian Linxweiler

Various cancer types including head and neck squamous cell carcinomas (HNSCC) show a frequent amplification of chromosomal region 3q26 that encodes, among others, for the SEC62 gene. Located in the ER membrane, this translocation protein is known to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdd83d6ae467fc0f30e5019fdca25d79

Mycolactone enhances the Ca2+ leakage from endoplasmic reticulum by trapping Sec61 translocons in a Ca2+ permeable state

Autor: S.J. Dos Santos, Richard Zimmermann, Pratiti Bhadra, Volkhard Helms, Adolfo Cavalié, Igor Gamayun, Tillman Pick, Rachel E. Simmonds, Belinda S. Hall, J. Ogbechi

The Mycobacterium ulcerans exotoxin, mycolactone, is an inhibitor of co-translational translocation via the Sec61 complex. Mycolactone has previously been shown to bind to, and alter the structure of, the major translocon subunit Sec61α, and change

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4f93494c31bd30dffd878696318b2d5f
https://doi.org/10.1101/2021.05.12.443793

Eeyarestatin 24 impairs SecYEG-dependent protein trafficking and inhibits growth of clinically relevant pathogens

Autor: Gregory Koningstein, Adolfo Cavalié, Julia Oswald, Joen Luirink, Maurice Steenhuis, Tillman Pick, Roger C. Whitehead, Sarah O'Keefe, Eileithyia Swanton, Hans-Georg Koch, Stephen High

Publikováno v: Molecular Microbiology, 115(1):32798330, 28-40. Wiley-Blackwell
Molecular Microbiology
Steenhuis, M, Koningstein, G M, Oswald, J, Pick, T, O’Keefe, S, Koch, H G, Cavalié, A, Whitehead, R C, Swanton, E, High, S & Luirink, J 2021, ' Eeyarestatin 24 impairs SecYEG-dependent protein trafficking and inhibits growth of clinically relevant pathogens ', Molecular Microbiology, vol. 115, no. 1, 32798330, pp. 28-40 . https://doi.org/10.1111/mmi.14589
Steenhuis, M, Koningstein, G M, Oswald, J, Pick, T, O'Keefe, S, Koch, H-G, Cavalie, A, Whitehead, R, Swanton, E, High, S & Luirink, J 2020, ' Eeyarestatin 24 Impairs SecYEG-dependent Protein Trafficking and Inhibits Growth of Clinically Relevant Pathogens ', Molecular Microbiology . https://doi.org/10.1111/mmi.14589

Eeyarestatin 1 (ES1) is an inhibitor of endoplasmic reticulum (ER) associated protein degradation, Sec61‐dependent Ca2+ homeostasis and protein translocation into the ER. Recently, evidence was presented showing that a smaller analog of ES1, ES24,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecf86b09944bd43755fd331784f1f6d7
https://research.vu.nl/en/publications/990f177a-afcd-4c8a-aaf0-8a5809e2d955