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Relevant bibliographies by topics / Myosin IIs - Bleb Dynamics

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Academic literature on the topic 'Myosin IIs - Bleb Dynamics'

Author: Grafiati

Published: 7 September 2023

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Journal articles on the topic "Myosin IIs - Bleb Dynamics"

1

Natarajan, Paramasivam, James M. Crothers, Jared E. Rosen, et al. "Myosin IIB and F-actin control apical vacuolar morphology and histamine-induced trafficking of H-K-ATPase-containing tubulovesicles in gastric parietal cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 306, no. 8 (2014): G699—G710. http://dx.doi.org/10.1152/ajpgi.00316.2013.

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Selective inhibitors of myosin or actin function and confocal microscopy were used to test the role of an actomyosin complex in controlling morphology, trafficking, and fusion of tubulovesicles (TV) containing H-K-ATPase with the apical secretory canaliculus (ASC) of primary-cultured rabbit gastric parietal cells. In resting cells, myosin IIB and IIC, ezrin, and F-actin were associated with ASC, whereas H-K-ATPase localized to intracellular TV. Histamine caused fusion of TV with ASC and subsequent expansion resulting from HCl and water secretion; F-actin and ezrin remained associated with ASC

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2

Asante-Asamani, Emmanuel, Derrick Brazill, and Wanda Strychalski. "Actin-myosin dynamics during bleb stabilization." Biophysical Journal 121, no. 3 (2022): 118a. http://dx.doi.org/10.1016/j.bpj.2021.11.2129.

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3

Park, Inju, Cecil Han, Sora Jin, et al. "Myosin regulatory light chains are required to maintain the stability of myosin II and cellular integrity." Biochemical Journal 434, no. 1 (2011): 171–80. http://dx.doi.org/10.1042/bj20101473.

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Myosin II is an actin-binding protein composed of MHC (myosin heavy chain) IIs, RLCs (regulatory light chains) and ELCs (essential light chains). Myosin II expressed in non-muscle tissues plays a central role in cell adhesion, migration and division. The regulation of myosin II activity is known to involve the phosphorylation of RLCs, which increases the Mg2+-ATPase activity of MHC IIs. However, less is known about the details of RLC–MHC II interaction or the loss-of-function phenotypes of non-muscle RLCs in mammalian cells. In the present paper, we investigate three highly conserved non-muscl

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4

Schiffhauer, Eric S., Yixin Ren, Vicente A. Iglesias, Priyanka Kothari, Pablo A. Iglesias, and Douglas N. Robinson. "Myosin IIB assembly state determines its mechanosensitive dynamics." Journal of Cell Biology 218, no. 3 (2019): 895–908. http://dx.doi.org/10.1083/jcb.201806058.

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Dynamical cell shape changes require a highly sensitive cellular system that can respond to chemical and mechanical inputs. Myosin IIs are key players in the cell’s ability to react to mechanical inputs, demonstrating an ability to accumulate in response to applied stress. Here, we show that inputs that influence the ability of myosin II to assemble into filaments impact the ability of myosin to respond to stress in a predictable manner. Using mathematical modeling for Dictyostelium myosin II, we predict that myosin II mechanoresponsiveness will be biphasic with an optimum established by the p

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5

Asante-Asamani, Emmanuel, Daniel Grange, Devarshi Rawal, Zully Santiago, John Loustau, and Derrick Brazill. "A role for myosin II clusters and membrane energy in cortex rupture for Dictyostelium discoideum." PLOS ONE 17, no. 4 (2022): e0265380. http://dx.doi.org/10.1371/journal.pone.0265380.

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Blebs, pressure driven protrusions of the cell membrane, facilitate the movement of eukaryotic cells such as the soil amoeba Dictyostelium discoideum, white blood cells and cancer cells. Blebs initiate when the cell membrane separates from the underlying cortex. A local rupture of the cortex, has been suggested as a mechanism by which blebs are initiated. However, much clarity is still needed about how cells inherently regulate rupture of the cortex in locations where blebs are expected to form. In this work, we examine the role of membrane energy and the motor protein myosin II (myosin) in fa

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