Results 31 to 40 of about 1,756,170 (285)

The Plasma Membrane Potential and the Organization of the Actin Cytoskeleton of Epithelial Cells

open access: yesInternational Journal of Cell Biology, 2012
The establishment and maintenance of the polarized epithelial phenotype require a characteristic organization of the cytoskeletal components. There are many cellular effectors involved in the regulation of the cytoskeleton of epithelial cells.
Silvia Chifflet, Julio A. Hernández
doaj   +1 more source

Catching a Walker in the Act—DNA Partitioning by ParA Family of Proteins

open access: yesFrontiers in Microbiology, 2022
Partitioning the replicated genetic material is a crucial process in the cell cycle program of any life form. In bacteria, many plasmids utilize cytoskeletal proteins that include ParM and TubZ, the ancestors of the eukaryotic actin and tubulin ...
Dipika Mishra   +3 more
doaj   +1 more source

Connecting two arrays: The emerging role of actin-microtubule cross-linking motor proteins

open access: yesFrontiers in Plant Science, 2015
The cytoskeleton of plant cells, consisting of actin filaments (AFs) and microtubules (MTs), is a central structure for various intracellular processes, such as cell division, isotropic and polar growth, vesicle transport, cell shape and morphogenesis ...
René eSchneider, Staffan ePersson
doaj   +1 more source

Cytoskeletal proteins: The evolution of cell division [PDF]

open access: yesCurrent Biology, 1998
The prokaryotic cell division protein FtsZ and eukaryotic tubulin have been shown to have very similar structures and are most likely homologs. The evolutionary transition from FtsZ to tubulin could provide a window into the transition from prokaryotic cells to eukaryotic cells.
Faguy, David M., Doolittle, W.Ford
openaire   +2 more sources

High-Frequency Irreversible Electroporation (H-FIRE) Induced Blood–Brain Barrier Disruption Is Mediated by Cytoskeletal Remodeling and Changes in Tight Junction Protein Regulation

open access: yesBiomedicines, 2022
Glioblastoma is the deadliest malignant brain tumor. Its location behind the blood–brain barrier (BBB) presents a therapeutic challenge by preventing effective delivery of most chemotherapeutics.
Brittanie R. Partridge   +10 more
doaj   +1 more source

Regulation of store-operated Ca2+ entry by Septins

open access: yesFrontiers in Cell and Developmental Biology, 2016
The mechanism of store-operated Ca2+entry (SOCE) brings extracellular Ca2+ into cells after depletion of intracellular Ca2+ stores. Regulation of Ca2+ homeostasis by SOCE helps control various intracellular signaling functions in both non-excitable and ...
Bipan Kumar Deb, Gaiti Hasan
doaj   +1 more source

Cytoskeletal Protein Variants Driving Atrial Fibrillation: Potential Mechanisms of Action

open access: yesCells, 2022
The most common clinical tachyarrhythmia, atrial fibrillation (AF), is present in 1–2% of the population. Although common risk factors, including hypertension, diabetes, and obesity, frequently underlie AF onset, it has been recognized that in 15% of the
Stan W. van Wijk   +4 more
doaj   +1 more source

Cellular levels of Grb2 and cytoskeleton stability are correlated in a neurodegenerative scenario

open access: yesDisease Models & Mechanisms, 2017
Alzheimer's disease (AD) manifests as neuronal loss. On the premise of Grb2 overexpression in AD mouse brain and brain tissues of AD patients, our study primarily focuses on the stability of cytoskeletal proteins in the context of degenerative AD-like ...
Piyali Majumder   +4 more
doaj   +1 more source

SHIP2 interaction with the cytoskeletal protein Vinexin [PDF]

open access: yesThe FEBS Journal, 2005
The src homology 2 (SH2) domain‐containing inositol 5‐phosphatase 2 (SHIP2) catalyses the dephosphorylation of phosphatidylinositol 3,4,5‐trisphosphate [PtdIns(3,4,5)P3] to phosphatidylinositol 3,4‐bisphosphate [PtdIns(3,4)P2]. We report the identification of the cytoskeletal protein Vinexin as a protein interacting with SHIP2.
Paternotte, Nathalie   +8 more
openaire   +3 more sources

An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane

open access: yesFEBS Letters, EarlyView.
Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa   +3 more
wiley   +1 more source

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