Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Nonmuscle Myosin Type IIB/metabolism"'
Autor:
Woroniuk, Anna, Porter, Andrew, White, Gavin, Newman, Daniel T., Diamantopoulou, Zoi, Waring, Thomas, Rooney, Claire, Strathdee, Douglas, Marston, Daniel J., Hahn, Klaus M., Sansom, Owen J., Zech, Tobias, Malliri, Angeliki
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Nature Communications
Woroniuk, A, Porter, A, White, G, Newman, D, Diamantopoulou, Z, Waring, T, Rooney, C, Strathdee, D, Marston, D J, Hahn, K M, Sansom, O J, Zech, T & Malliri, A 2018, ' STEF/TIAM2 mediated Rac1 activity at the nuclear envelope regulates the perinuclear actin cap ', Nature Communications, vol. 9, no. 1, 2124 . https://doi.org/10.1038/s41467-018-04404-4
Nature Communications
Woroniuk, A, Porter, A, White, G, Newman, D, Diamantopoulou, Z, Waring, T, Rooney, C, Strathdee, D, Marston, D J, Hahn, K M, Sansom, O J, Zech, T & Malliri, A 2018, ' STEF/TIAM2 mediated Rac1 activity at the nuclear envelope regulates the perinuclear actin cap ', Nature Communications, vol. 9, no. 1, 2124 . https://doi.org/10.1038/s41467-018-04404-4
The perinuclear actin cap is an important cytoskeletal structure that regulates nuclear morphology and re-orientation during front-rear polarisation. The mechanisms regulating the actin cap are currently poorly understood. Here, we demonstrate that S
Autor:
Inês Mendes Pinto, Diana Machado, David Rosa, Ana Costa, Ana Catarina Costa, Paula Sampaio, Marko Lampe, Feng Quan Zhou, Cátia D. F. Lopes, Paulo Aguiar, Rita Pinto-Costa, Luis Pajuelo, Xuewei Wang, Boris Rubinstein, Mónica Mendes Sousa, Sara C. Sousa, António J. Pereira, José C. Mateus
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
Neurons have a membrane periodic skeleton (MPS) composed of actin rings interconnected by spectrin. Here, combining chemical and genetic gain- and loss-of-function assays, we show that in rat hippocampal neurons the MPS is an actomyosin network that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e20d137be9429c4b64183418c4883241
https://hdl.handle.net/10216/141444
https://hdl.handle.net/10216/141444
Publikováno v:
Molecular biology of the cell. 18(3):1009-1017
To function in the cell, nonmuscle myosin II molecules assemble into filaments through their C-terminal tails. Because myosin II isoforms most likely assemble into homo-filaments in vivo, it seems that some self-recognition mechanisms of individual m