Výsledky vyhledávání - "Sarah J. Copeland"

Actin-dependent regulation of cilia length by the inverted formin FHDC1

Autor: John W. Copeland, Andrea McRae, Giulia Guarguaglini, Laura Trinkle-Mulcahy, Sarah J. Copeland

Publikováno v: Molecular biology of the cell 29 (2018): 1611–1627. doi:10.1091/mbc.E18-02-0088
info:cnr-pdr/source/autori:Copeland S.J.; McRae A.; Guarguaglini G.; Trinkle-Mulcahy L.; Copeland J.W./titolo:Actin-dependent regulation of cilia length by the inverted formin FHDC1/doi:10.1091%2Fmbc.E18-02-0088/rivista:Molecular biology of the cell/anno:2018/pagina_da:1611/pagina_a:1627/intervallo_pagine:1611–1627/volume:29

A primary cilium is found on most mammalian cells, where it acts as a cellular antenna for the reception of both mechanical and chemical signals. A variety of diseases are associated with defective ciliogenesis, reflecting the ubiquity of the functio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30ba9464f8cf83182923e1217ada876c
https://doi.org/10.1091/mbc.e18-02-0088

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Actin- and microtubule-dependent regulation of Golgi morphology by FHDC1

Autor: John W. Copeland, Sarah J. Copeland, Susan F. Thurston

Publikováno v: Molecular Biology of the Cell

The coordinated action of the actin and microtubule cytoskeletal networks is required for Golgi ribbon assembly. The novel formin FHDC1 accumulates on the Golgi-derived microtubule network, where it acts to regulate Golgi ribbon assembly in an actin-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f712fe5c1af93422cd137393472978f5
https://doi.org/10.1091/mbc.e15-02-0070

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Pseudomonas aeruginosa Biofilm Antibiotic Resistance Gene ndvB Expression Requires the RpoS Stationary-Phase Sigma Factor

Autor: Bratati Saha, Aaron Hinz, Sarah J. Copeland, Li Zhang, Jean-Paul Nadeau, Thien-Fah Mah, Clayton W. Hall, Luke B.-P. Gagnon

Publikováno v: Applied and Environmental Microbiology. 84

Chronic, biofilm-based bacterial infections are exceptionally difficult to eradicate due to the high degree of antibiotic recalcitrance exhibited by cells in biofilm communities. In the opportunistic pathogen Pseudomonas aeruginosa , biofilm recalcit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e60e9a1fbac818e6bf0b610c38f6e5a0
https://doi.org/10.1128/aem.02762-17

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A specific FMNL2 isoform is up-regulated in invasive cells

Autor: Melissa T. Maltez, Allan Heibein, Christine Péladeau, John W. Copeland, Sarah J. Copeland

Publikováno v: BMC Cell Biology

Background Formins are a highly conserved family of cytoskeletal remodeling proteins. A growing body of evidence suggests that formins play key roles in the progression and spread of a variety of cancers. There are 15 human formin proteins and of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdba45f0413ca6ae9dd62ee2d0e6deef
https://pubmed.ncbi.nlm.nih.gov/27578625

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INF1 Is a Novel Microtubule-associated Formin

Autor: Chelsea Smallwood, John W. Copeland, Sarah J. Copeland, Susan F. Thurston, Kevin G. Young

Publikováno v: Molecular Biology of the Cell. 19:5168-5180

Formin proteins, characterized by the presence of conserved formin homology (FH) domains, play important roles in cytoskeletal regulation via their abilities to nucleate actin filament formation and to interact with multiple other proteins involved i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe23cdaa60f46ba87a9b8062dffd900f
https://doi.org/10.1091/mbc.e08-05-0469

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Interaction of the N- and C-terminal Autoregulatory Domains of FRL2 Does Not Inhibit FRL2 Activity

Autor: Sarah J. Copeland, Nezar Abdennur, Dominique C. Vaillant, John W. Copeland, Chris Davis, Susan F. Thurston

Publikováno v: Journal of Biological Chemistry. 283:33750-33762

Formin homology proteins are a highly conserved family of cytoskeletal remodeling proteins best known for their ability to induce the formation of long unbranched actin filaments. They accomplish this by nucleating the de novo polymerization of F-act

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40f17348cbf3abf5f2a5085b178ee88e
https://doi.org/10.1074/jbc.m803156200

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The Diaphanous Inhibitory Domain/Diaphanous Autoregulatory Domain Interaction Is Able to Mediate Heterodimerization between mDia1 and mDia2

Autor: Sarah Burchat, Brenda J. Green, Giuseppe A. Papalia, John W. Copeland, David Banner, Sarah J. Copeland

Publikováno v: Journal of Biological Chemistry. 282:30120-30130

Formins are multidomain proteins that regulate numerous cytoskeleton-dependent cellular processes. These effects are mediated by the presence of two regions of homology, formin homology 1 and FH2. The diaphanous-related formins (DRFs) are distinguish

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::def27106dc9eebd093d98951151595cc
https://doi.org/10.1074/jbc.m703834200

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Homo-oligomerization is essential for F-actin assembly by the formin family FH2 domain

Autor: Sarah J. Copeland, Richard Treisman, John W. Copeland

Publikováno v: The Journal of biological chemistry. 279(48)

Formin proteins regulate the actin and microtubule cytoskeletons and also control the activity of the SRF transcription factor through depletion of the G-actin pool. Although the conserved formin homology 2 (FH2) domains of the mDia1 and Bni1 formins

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a4ea74bd95c8e68710b552a1c6f74b8
https://pubmed.ncbi.nlm.nih.gov/15371418

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