Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Isabelle, Méan"'
Publikováno v:
Cells, Vol 12, Iss 15, p 2004 (2023)
Cingulin (CGN) and paracingulin (CGNL1) are cytoplasmic proteins of tight junctions (TJs), where they play a role in tethering ZO-1 to the actomyosin and microtubule cytoskeletons. The role of CGN and CGNL1 in the barrier function of epithelia is not
Externí odkaz:
https://doaj.org/article/83ba493373054e84aec8d6b4ed257a67
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
PLEKHA5, PLEKHA6, and PLEKHA7 (WW-PLEKHAs) are members of the PLEKHA family of proteins that interact with PDZD11 through their tandem WW domains. WW-PLEKHAs contribute to the trafficking and retention of transmembrane proteins, including nectins, Ts
Externí odkaz:
https://doaj.org/article/1b51ff394f3847219f63468f51452a64
Publikováno v:
Cells, Vol 11, Iss 4, p 627 (2022)
Transmembrane proteins of adherens and tight junctions are known targets for viruses and bacterial toxins. The coronavirus receptor ACE2 has been localized at the apical surface of epithelial cells, but it is not clear whether ACE2 is localized at ap
Externí odkaz:
https://doaj.org/article/f23625556fbe4dabba761aa568f8e28e
Autor:
Florian Rouaud, Wenmao Huang, Arielle Flinois, Kunalika Jain, Ekaterina Vasileva, Thomas Di Mattia, Marine Mauperin, David A.D. Parry, Vera Dugina, Christine Chaponnier, Isabelle Méan, Sylvie Montessuit, Annick Mutero-Maeda, Jie Yan, Sandra Citi
Publikováno v:
Journal of Cell Biology. 222
The mechanisms that regulate the spatial sorting of nonmuscle myosins-2 (NM2) isoforms and couple them mechanically to the plasma membrane are unclear. Here we show that the cytoplasmic junctional proteins cingulin (CGN) and paracingulin (CGNL1) inte
Publikováno v:
Journal of Cell Science. 137
Paracingulin (CGNL1) is recruited to tight junctions (TJs) by ZO-1 and to adherens junctions (AJs) by PLEKHA7. PLEKHA7 has been reported to bind to the microtubule minus-end-binding protein CAMSAP3, to tether microtubules to the AJs. Here, we show th
Publikováno v:
Cells; Volume 11; Issue 4; Pages: 627
Transmembrane proteins of adherens and tight junctions are known targets for viruses and bacterial toxins. The coronavirus receptor ACE2 has been localized at the apical surface of epithelial cells, but it is not clear whether ACE2 is localized at ap
Autor:
Ekaterina, Vasileva, Domenica, Spadaro, Florian, Rouaud, Jonathan M, King, Arielle, Flinois, Jimit, Shah, Sophie, Sluysmans, Isabelle, Méan, Lionel, Jond, Jerrold R, Turner, Sandra, Citi
Publikováno v:
The Journal of biological chemistry. 298(4)
Zonula occludens-1 (ZO-1), the major scaffolding protein of tight junctions (TJs), recruits the cytoskeleton-associated proteins cingulin (CGN) and paracingulin (CGNL1) to TJs by binding to their N-terminal ZO-1 interaction motif. The conformation of
Autor:
Isabelle Méan, Sandra Citi, Sophie Sluysmans, F. Ferreira, Tong Xiao, Chunmei Chang, A. Boukhatemi, Lionel Jond
Copper homeostasis is crucial for cellular physiology and development, and its dysregulation leads to disease. The Menkes ATPase ATP7A plays a key role in copper efflux, by trafficking from the Golgi to the plasma membrane upon cell exposure to eleva
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3335d46b40cd06d1b386aada808d9219
https://doi.org/10.1101/2021.06.17.448791
https://doi.org/10.1101/2021.06.17.448791
Autor:
Lionel Jond, Flavio Ferreira, Tong Xiao, Sophie Sluysmans, Christopher J. Chang, Isabelle Méan, Sandra Citi, Annick Mutero, Amina Boukhatemi
Publikováno v:
Molecular biology of the cell, Vol. 32, No 21 (2021)
Molecular biology of the cell, vol 32, iss 21
Molecular Biology of the Cell
Molecular biology of the cell, vol 32, iss 21
Molecular Biology of the Cell
Copper homeostasis is crucial for cellular physiology and development, and its dysregulation leads to disease. The Menkes ATPase ATP7A plays a key role in copper efflux, by trafficking from the Golgi to the plasma membrane upon cell exposure to eleva
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::162d652b4e71471d72728f95fbb00b2e
https://archive-ouverte.unige.ch/unige:158431
https://archive-ouverte.unige.ch/unige:158431