Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Heike Nägele"'
Autor:
Arunas Kvainickas, Florian Steinberg, Wenjing Qi, Ana Jimenez-Orgaz, Jörn Dengjel, Luca H. Stehl, Heike Nägele, Zehan Hu, Claudio De Virgilio, Ralf Baumeister, Qian Zhao, Ladislav Dokládal, Dipak Gangurde
Publikováno v:
The Journal of Cell Biology
Kvainickas et al. establish that retromer, a coat complex that promotes endosomal recycling, is also required for the activation of the lysosomal mTORC1 complex. Mechanistically, retromer and the retromer-associated protein TBC1D5 separate mTORC1 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8122b7026817320c2fb63e7b1ffd24fd
https://doi.org/10.1083/jcb.201812110
https://doi.org/10.1083/jcb.201812110
Autor:
Stefan Eimer, Ana Jimenez-Orgaz, Heike Nägele, Florian Steinberg, Arunas Kvainickas, Justin Denner, Jörn Dengjel
Publikováno v:
The EMBO Journal
Retromer is an endosomal multi‐protein complex that organizes the endocytic recycling of a vast range of integral membrane proteins. Here, we establish an additional retromer function in controlling the activity and localization of the late endosom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6971fdc53a88488565629d76c513cc20
https://doi.org/10.15252/embj.201797128
https://doi.org/10.15252/embj.201797128
Autor:
Lindsey L. Morris, Lawrence Banks, David Pim, Paul F. Langton, Amika Singla, Neil D. Pearson, Rebecca A. Faulkner, Kerrie E. McNally, Ezra Burstein, Chris M. Danson, Richard B. Sessions, Matthew Gallon, Rajesh Ghai, Brittany L. Overlee, Brett M. Collins, Heike Nägele, Imre Berger, Daniel D. Billadeau, Peter J. Cullen, Kate J. Heesom, Florian Steinberg
Publikováno v:
McNally, K E, Faulkner, R, Steinberg, F, Gallon, M, Ghai, R, Pim, D, Langton, P, Pearson, N, Danson, C M, Nägele, H, Morris, L L, Singla, A, Overlee, B L, Heesom, K J, Sessions, R, Banks, L, Collins, B M, Berger, I, Billadeau, D D, Burstein, E & Cullen, P J 2017, ' Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling ', Nature Cell Biology, vol. 19, no. 10, pp. 1214–1225 . https://doi.org/10.1038/ncb3610
Following endocytosis into the endosomal network, integral membrane proteins undergo sorting for lysosomal degradation or are retrieved and recycled back to the cell surface. Here we describe the discovery of an ancient and conserved multiprotein com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5c857598e82e04766549d6478540a96
https://doi.org/10.1038/ncb3610
https://doi.org/10.1038/ncb3610
Autor:
Ana Jimenez Orgaz, Arunas Kvainickas, Kate J. Heesom, Jörn Dengjel, Florian Steinberg, Heike Nägele, Britta Diedrich, Peter J. Cullen
Publikováno v:
Kvainickas, A, Jimenez Orgaz, A, Nägele, H, Diedrich, B, Heesom, K, Dengjel, J, Cullen, P & Steinberg, F 2017, ' Retromer/WASH dependent sorting of nutrient transporters requires a multivalent interaction network with ANKRD50 ', Journal of Cell Science, vol. 130, pp. 382-395 . https://doi.org/10.1242/jcs.196758, https://doi.org/10.1242/jcs.196758
Retromer and the associated actin-polymerizing WASH complex are essential for the endocytic recycling of a wide range of integral membrane proteins. A hereditary Parkinson's-disease-causing point mutation (D620N) in the retromer subunit VPS35 perturb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95a525dca08ff35e111b8db1e36ea512
http://doc.rero.ch/record/288525/files/den_rwd.pdf
http://doc.rero.ch/record/288525/files/den_rwd.pdf
Autor:
Arunas Kvainickas, Heike Nägele, Jörn Dengjel, Zehan Hu, Ana Jimenez-Orgaz, Florian Steinberg
Publikováno v:
The Journal of Cell Biology
Kvainickas et al. show that the retromer cargo CI-MPR does not recycle from endosomes to the trans-Golgi network through interactions with the core retromer trimer. Instead, CI-MPR depends on cargo-selective SNX-BAR proteins, which function independe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdd16c58cebcc6c63c2406de4cb99f2a
https://pubmed.ncbi.nlm.nih.gov/29061649
https://pubmed.ncbi.nlm.nih.gov/29061649