scholarly journals Two timescales control the creation of large protein aggregates in cells

2021 ◽  
Author(s):  
Ander Movilla Miangolarra ◽  
Aleria Duperray-Susini ◽  
Mathieu Coppey ◽  
Michele Castellana
Keyword(s):  
Protein Aggregation ◽  
Pore Size ◽  
Cell Biology ◽  
Spatial Organization ◽  
Aggregation Process ◽  
Large Protein ◽  
Random Forces ◽  
Small Clusters ◽  
Slow Timescale ◽  
In Cells

Protein aggregation is of particular interest due to its connection with many diseases and disorders. Many factors can alter the dynamics and result of this process, one of them being the diffusivity of the monomers and aggregates in the system. Here, we study experimentally and theoretically an aggregation process in cells, and we identify two distinct physical timescales that set the number and size of aggregates. The first timescale involves fast aggregation of small clusters freely diffusing in the cytoplasm, while, in the second one, the aggregates are larger than the pore size of the cytoplasm and thus barely diffuse, and the aggregation process is slowed down. However, the process is not entirely halted, potentially reflecting a myriad of active but random forces forces that stir the aggregates. Such slow timescale is essential to account for the experimental results of the aggregation process. These results could also have implications in other processes of spatial organization in cell biology, such as phase-separated droplets.

scholarly journals Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2371
Author(s):  
Valeria Guarrasi ◽  
Giacoma Cinzia Rappa ◽  
Maria Assunta Costa ◽  
Fabio Librizzi ◽  
Marco Raimondo ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Environmental Sustainability ◽  
Bovine Milk ◽  
Amyloid Formation ◽  
Aggregation Process ◽  
Amyloid Aggregation ◽  
Social Challenges ◽  
Force Microscopy ◽  
Atomic Force ◽  
Apple Peels

Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of κ-casein from bovine milk, a well-used amyloidogenic model system. The effect of the apple peel extract on protein aggregation was examined using a thioflavin T fluorescence assay, Congo red binding assay, circular dichroism, light scattering, and atomic force microscopy. We found that the phenolic extract from the peel of apples of the cultivar “Fuji”, cultivated in Sicily (Caltavuturo, Italy), inhibited κ-casein fibril formation in a dose-dependent way. In particular, we found that the extract significantly reduced the protein aggregation rate and inhibited the secondary structure reorganization that accompanies κ-casein amyloid formation. Protein-aggregated species resulting from the incubation of κ-casein in the presence of polyphenols under amyloid aggregation conditions were reduced in number and different in morphology.

scholarly journals 3P189 Movement of nucleus in cells cultured on micro-patterned substrates(Cell biology,Poster,The 52th Annual Meeting of the Biophysical Society of Japan(BSJ2014))

2014 ◽  
Vol 54 (supplement1-2) ◽  
pp. S280
Author(s):  
Zhu Xinfeng ◽  
Kuribayashi-Shigetomi Kaori ◽  
Cai Pinggen ◽  
Subagyo Agus ◽  
Sueoka Kazuhisa ◽  
...  
Keyword(s):  
Annual Meeting ◽  
Cell Biology ◽  
Patterned Substrates ◽  
Biophysical Society ◽  
Cells Cultured ◽  
In Cells

scholarly journals Tracking protein aggregation and mislocalization in cells with flow cytometry

2012 ◽  
Vol 9 (5) ◽  
pp. 467-470 ◽  
Author(s):  
Yasmin M Ramdzan ◽  
Saskia Polling ◽  
Cheryl P Z Chia ◽  
Ivan H W Ng ◽  
Angelique R Ormsby ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Protein Aggregation ◽  
In Cells

scholarly journals Amyloid-like aggregating proteins cause lysosomal defects in neurons via gain-of-function toxicity

2021 ◽  
Vol 5 (3) ◽  
pp. e202101185
Author(s):  
Irene Riera-Tur ◽  
Tillman Schäfer ◽  
Daniel Hornburg ◽  
Archana Mishra ◽  
Miguel da Silva Padilha ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Protein Trafficking ◽  
Cell Biology ◽  
Electron Tomography ◽  
Lysosomal Storage ◽  
Gain Of Function ◽  
Cryo Electron Tomography ◽  
A Subunit ◽  
Late Stages ◽  
Β Sheet

The autophagy-lysosomal pathway is impaired in many neurodegenerative diseases characterized by protein aggregation, but the link between aggregation and lysosomal dysfunction remains poorly understood. Here, we combine cryo-electron tomography, proteomics, and cell biology studies to investigate the effects of protein aggregates in primary neurons. We use artificial amyloid-like β-sheet proteins (β proteins) to focus on the gain-of-function aspect of aggregation. These proteins form fibrillar aggregates and cause neurotoxicity. We show that late stages of autophagy are impaired by the aggregates, resulting in lysosomal alterations reminiscent of lysosomal storage disorders. Mechanistically, β proteins interact with and sequester AP-3 μ1, a subunit of the AP-3 adaptor complex involved in protein trafficking to lysosomal organelles. This leads to destabilization of the AP-3 complex, missorting of AP-3 cargo, and lysosomal defects. Restoring AP-3μ1 expression ameliorates neurotoxicity caused by β proteins. Altogether, our results highlight the link between protein aggregation, lysosomal impairments, and neurotoxicity.

scholarly journals Emerin modulates spatial organization of chromosome territories in cells on softer matrices

2018 ◽  
Vol 46 (11) ◽  
pp. 5561-5586 ◽  
Author(s):  
Roopali Pradhan ◽  
Devika Ranade ◽  
Kundan Sengupta
Keyword(s):  
Spatial Organization ◽  
Chromosome Territories ◽  
In Cells

scholarly journals Cas3 Protein—A Review of a Multi-Tasking Machine

Genes ◽  
2020 ◽  
Vol 11 (2) ◽  
pp. 208 ◽  
Author(s):  
Liu He ◽  
Michael St. John James ◽  
Marin Radovcic ◽  
Ivana Ivancic-Bace ◽  
Edward L. Bolt
Keyword(s):  
Cell Biology ◽  
Protein A ◽  
Mobile Genetic Elements ◽  
Genetic Elements ◽  
Cellular Processes ◽  
Concise Review ◽  
In Cells

Cas3 has essential functions in CRISPR immunity but its other activities and roles, in vitro and in cells, are less widely known. We offer a concise review of the latest understanding and questions arising from studies of Cas3 mechanism during CRISPR immunity, and highlight recent attempts at using Cas3 for genetic editing. We then spotlight involvement of Cas3 in other aspects of cell biology, for which understanding is lacking—these focus on CRISPR systems as regulators of cellular processes in addition to defense against mobile genetic elements.

Imaging myosin 10 in cells

2004 ◽  
Vol 32 (5) ◽  
pp. 689-693 ◽  
Author(s):  
D. Tacon ◽  
P.J. Knight ◽  
M. Peckham
Keyword(s):  
Green Fluorescent Protein ◽  
Cell Biology ◽  
Fluorescent Protein ◽  
Major Task ◽  
Green Fluorescent ◽  
In Cells

Cellular motors (kinesin, dynein and myosin) are ubiquitous. A major task in cell biology is to determine how they function in cells. Here we focus on myosin 10, an intrafilopodial motor, and show how imaging green fluorescent protein fused to myosin 10 or its tail domains can help us understand the function of this myosin.

Protein aggregation in cell biology: An aggregomics perspective of health and disease

2020 ◽  
Vol 99 ◽  
pp. 40-54 ◽  
Author(s):  
Dezerae Cox ◽  
Candice Raeburn ◽  
Xiaojing Sui ◽  
Danny M. Hatters
Keyword(s):  
Protein Aggregation ◽  
Cell Biology ◽  
Health And Disease
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