Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Ellen J. Ezratty"'
Publikováno v:
Molecular Biology of the Cell
Directional cell migration drives embryonic development, cancer metastasis, and tissue repair and regeneration. Here, we examine the role of intraflagellar transport (IFT) 20 (Ift20) during polarized migration of epidermal cells. IFT20 is implicated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6655c376d5781fc8c924d7cb025a4b9
https://doi.org/10.1091/mbc.e20-04-0232
https://doi.org/10.1091/mbc.e20-04-0232
Publikováno v:
Development
Arl/ARF GTPases regulate ciliary trafficking, but their tissue-specific functions are unclear. Here, we demonstrate that ciliary GTPase Arl3 is required for mitotic spindle orientation of mouse basal stem cells during skin development. Arl3 loss dimi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cdba1c9602b9f80d9a94c868eea5a39
https://doi.org/10.1242/dev.161885
https://doi.org/10.1242/dev.161885
Publikováno v:
Journal of Cell Science. 129:1525-1529
In the city that never sleeps, great science never takes a break. On 15 January 2016, the ‘New York Symposium on Quantitative Biology of the Cell’, a one-day local meeting of the American Society for Cell Biology (ASCB), took place at Columbia Un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::63c5a39eec5fe42d78d546f036a24729
https://doi.org/10.1242/jcs.188375
https://doi.org/10.1242/jcs.188375
Publikováno v:
Nature Cell Biology. 18:491-503
Integrin endocytic recycling is critical for cell migration, yet how recycled integrins assemble into new adhesions is unclear. By synchronizing endocytic disassembly of focal adhesions (FAs), we find that recycled integrins reassemble FAs coincident
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7317011c0689cb225de86036ed7018b0
https://doi.org/10.1038/ncb3333
https://doi.org/10.1038/ncb3333
Publikováno v:
The Journal of Cell Biology
A new mechanism for focal adhesion disassembly is described involving microtubule-stimulated endocytosis of integrins at focal adhesions.
Focal adhesion disassembly is regulated by microtubules (MTs) through an unknown mechanism that involves dy
Focal adhesion disassembly is regulated by microtubules (MTs) through an unknown mechanism that involves dy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c9aa91f14b4ad7b7061b4f1e2e00e1a
https://doi.org/10.1083/jcb.200904054
https://doi.org/10.1083/jcb.200904054
Publikováno v:
The Journal of Cell Biology
Ciliogenesis in differentiating epidermal cells correlates with activation of Notch signaling, which requires Presenilin-2 targeting to basal bodies/cilia. Ezratty et al. show that the GTPase ARF4 regulates Presenilin-2 localization and subsequent No
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::126ae346fa247c66ca48a8859f137a7c
https://pubmed.ncbi.nlm.nih.gov/27354375
https://pubmed.ncbi.nlm.nih.gov/27354375
Autor:
Michael A. Partridge, Eugene E. Marcantonio, Myeong Gu Yeo, Qiong Shen, Gregg G. Gundersen, Ellen J. Ezratty
Publikováno v:
Molecular and Cellular Biology. 26:4399-4409
Src kinase is a crucial mediator of adhesion-related signaling and motility. Src binds to focal adhesion kinase (FAK) through its SH2 domain and subsequently activates it for phosphorylation of downstream substrates. In addition to this binding funct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bf123c34d57967209da34f32ae17b5a
https://doi.org/10.1128/mcb.01147-05
https://doi.org/10.1128/mcb.01147-05
Publikováno v:
Nature cell biology. 7(6)
Imaging studies implicate microtubule targeting of focal adhesions in focal adhesion disassembly, although the molecular mechanism is unknown. Here, we develop a model system of focal adhesion disassembly based on the finding that microtubule regrowt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bec78b70dbfbb2a8d26fff7a74885dfd
https://pubmed.ncbi.nlm.nih.gov/15928699
https://pubmed.ncbi.nlm.nih.gov/15928699