Macromolecular crowding: Sensing without a sensor
Curr Opin Cell Biol. 2023 Oct 26;85:102269. doi: 10.1016/j.ceb.2023.102269. Online ahead of print.ABSTRACTAll living cells are crowded with macromolecules. Crowding can directly modulate biochemical reactions to various degrees depending on the sizes, shapes, and binding affinities of the reactants. Here, we explore the possibility that cells can sense and adapt to changes in crowding through the widespread modulation of biochemical reactions without the need for a dedicated sensor. Additionally, we explore phase separation as a general physicochemical response to changes in crowding, and a mechanism to both transduce info...
Source: Current Opinion in Cell Biology - October 28, 2023 Category: Cytology Authors: Liam J Holt Morgan Delarue Source Type: research
Live-cell imaging in the deep learning era
Curr Opin Cell Biol. 2023 Oct 26;85:102271. doi: 10.1016/j.ceb.2023.102271. Online ahead of print.ABSTRACTLive imaging is a powerful tool, enabling scientists to observe living organisms in real time. In particular, when combined with fluorescence microscopy, live imaging allows the monitoring of cellular components with high sensitivity and specificity. Yet, due to critical challenges (i.e., drift, phototoxicity, dataset size), implementing live imaging and analyzing the resulting datasets is rarely straightforward. Over the past years, the development of bioimage analysis tools, including deep learning, is changing how w...
Source: Current Opinion in Cell Biology - October 28, 2023 Category: Cytology Authors: Joanna W Pylv änäinen Estibaliz G ómez-de-Mariscal Ricardo Henriques Guillaume Jacquemet Source Type: research
Macromolecular crowding: Sensing without a sensor
Curr Opin Cell Biol. 2023 Oct 26;85:102269. doi: 10.1016/j.ceb.2023.102269. Online ahead of print.ABSTRACTAll living cells are crowded with macromolecules. Crowding can directly modulate biochemical reactions to various degrees depending on the sizes, shapes, and binding affinities of the reactants. Here, we explore the possibility that cells can sense and adapt to changes in crowding through the widespread modulation of biochemical reactions without the need for a dedicated sensor. Additionally, we explore phase separation as a general physicochemical response to changes in crowding, and a mechanism to both transduce info...
Source: Current Opinion in Cell Biology - October 28, 2023 Category: Cytology Authors: Liam J Holt Morgan Delarue Source Type: research
The unique biomechanics of intermediate filaments - From single filaments to cells and tissues
Curr Opin Cell Biol. 2023 Oct 21;85:102263. doi: 10.1016/j.ceb.2023.102263. Online ahead of print.ABSTRACTTogether with actin filaments and microtubules, intermediate filaments (IFs) constitute the eukaryotic cytoskeleton and each of the three filament types contributes very distinct mechanical properties to this intracellular biopolymer network. IFs assemble hierarchically, rather than polymerizing from nuclei of a small number of monomers or dimers, as is the case with actin filaments and microtubules, respectively. This pathway leads to a molecular architecture specific to IFs and intriguing mechanical and dynamic prope...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Ulrike R ölleke Pallavi Kumari Ruth Meyer Sarah K öster Source Type: research
Lamins as structural nuclear elements through evolution
Curr Opin Cell Biol. 2023 Oct 21;85:102267. doi: 10.1016/j.ceb.2023.102267. Online ahead of print.ABSTRACTLamins are nuclear intermediate filament proteins with important, well-established roles in humans and other vertebrates. Lamins interact with DNA and numerous proteins at the nuclear envelope to determine the mechanical properties of the nucleus, coordinate chromatin organization, and modulate gene expression. Many of these functions are conserved in the lamin homologs found in basal metazoan organisms, including Drosophila and Caenorhabditis elegans. Lamin homologs have also been recently identified in non-metazoans,...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Jacob Odell Jan Lammerding Source Type: research
How do disordered head domains assist in the assembly of intermediate filaments?
Curr Opin Cell Biol. 2023 Oct 21;85:102262. doi: 10.1016/j.ceb.2023.102262. Online ahead of print.ABSTRACTThe dominant structural feature of intermediate filament (IF) proteins is a centrally located α-helix. These long α-helical segments become paired in a parallel orientation to form coiled-coil dimers. Pairs of dimers further coalesce in an anti-parallel orientation to form tetramers. These early stages of intermediate filament assembly can be accomplished solely by the central α-helices. By contrast, the assembly of tetramers into mature intermediate filaments is reliant upon an N-terminal head domain. IF head domai...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Xiaoming Zhou Masato Kato Steven L McKnight Source Type: research
The unique biomechanics of intermediate filaments - From single filaments to cells and tissues
Curr Opin Cell Biol. 2023 Oct 21;85:102263. doi: 10.1016/j.ceb.2023.102263. Online ahead of print.ABSTRACTTogether with actin filaments and microtubules, intermediate filaments (IFs) constitute the eukaryotic cytoskeleton and each of the three filament types contributes very distinct mechanical properties to this intracellular biopolymer network. IFs assemble hierarchically, rather than polymerizing from nuclei of a small number of monomers or dimers, as is the case with actin filaments and microtubules, respectively. This pathway leads to a molecular architecture specific to IFs and intriguing mechanical and dynamic prope...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Ulrike R ölleke Pallavi Kumari Ruth Meyer Sarah K öster Source Type: research
Lamins as structural nuclear elements through evolution
Curr Opin Cell Biol. 2023 Oct 21;85:102267. doi: 10.1016/j.ceb.2023.102267. Online ahead of print.ABSTRACTLamins are nuclear intermediate filament proteins with important, well-established roles in humans and other vertebrates. Lamins interact with DNA and numerous proteins at the nuclear envelope to determine the mechanical properties of the nucleus, coordinate chromatin organization, and modulate gene expression. Many of these functions are conserved in the lamin homologs found in basal metazoan organisms, including Drosophila and Caenorhabditis elegans. Lamin homologs have also been recently identified in non-metazoans,...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Jacob Odell Jan Lammerding Source Type: research
How do disordered head domains assist in the assembly of intermediate filaments?
Curr Opin Cell Biol. 2023 Oct 21;85:102262. doi: 10.1016/j.ceb.2023.102262. Online ahead of print.ABSTRACTThe dominant structural feature of intermediate filament (IF) proteins is a centrally located α-helix. These long α-helical segments become paired in a parallel orientation to form coiled-coil dimers. Pairs of dimers further coalesce in an anti-parallel orientation to form tetramers. These early stages of intermediate filament assembly can be accomplished solely by the central α-helices. By contrast, the assembly of tetramers into mature intermediate filaments is reliant upon an N-terminal head domain. IF head domai...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Xiaoming Zhou Masato Kato Steven L McKnight Source Type: research
The unique biomechanics of intermediate filaments - From single filaments to cells and tissues
Curr Opin Cell Biol. 2023 Oct 21;85:102263. doi: 10.1016/j.ceb.2023.102263. Online ahead of print.ABSTRACTTogether with actin filaments and microtubules, intermediate filaments (IFs) constitute the eukaryotic cytoskeleton and each of the three filament types contributes very distinct mechanical properties to this intracellular biopolymer network. IFs assemble hierarchically, rather than polymerizing from nuclei of a small number of monomers or dimers, as is the case with actin filaments and microtubules, respectively. This pathway leads to a molecular architecture specific to IFs and intriguing mechanical and dynamic prope...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Ulrike R ölleke Pallavi Kumari Ruth Meyer Sarah K öster Source Type: research
Lamins as structural nuclear elements through evolution
Curr Opin Cell Biol. 2023 Oct 21;85:102267. doi: 10.1016/j.ceb.2023.102267. Online ahead of print.ABSTRACTLamins are nuclear intermediate filament proteins with important, well-established roles in humans and other vertebrates. Lamins interact with DNA and numerous proteins at the nuclear envelope to determine the mechanical properties of the nucleus, coordinate chromatin organization, and modulate gene expression. Many of these functions are conserved in the lamin homologs found in basal metazoan organisms, including Drosophila and Caenorhabditis elegans. Lamin homologs have also been recently identified in non-metazoans,...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Jacob Odell Jan Lammerding Source Type: research
How do disordered head domains assist in the assembly of intermediate filaments?
Curr Opin Cell Biol. 2023 Oct 21;85:102262. doi: 10.1016/j.ceb.2023.102262. Online ahead of print.ABSTRACTThe dominant structural feature of intermediate filament (IF) proteins is a centrally located α-helix. These long α-helical segments become paired in a parallel orientation to form coiled-coil dimers. Pairs of dimers further coalesce in an anti-parallel orientation to form tetramers. These early stages of intermediate filament assembly can be accomplished solely by the central α-helices. By contrast, the assembly of tetramers into mature intermediate filaments is reliant upon an N-terminal head domain. IF head domai...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Xiaoming Zhou Masato Kato Steven L McKnight Source Type: research
The unique biomechanics of intermediate filaments - From single filaments to cells and tissues
Curr Opin Cell Biol. 2023 Oct 21;85:102263. doi: 10.1016/j.ceb.2023.102263. Online ahead of print.ABSTRACTTogether with actin filaments and microtubules, intermediate filaments (IFs) constitute the eukaryotic cytoskeleton and each of the three filament types contributes very distinct mechanical properties to this intracellular biopolymer network. IFs assemble hierarchically, rather than polymerizing from nuclei of a small number of monomers or dimers, as is the case with actin filaments and microtubules, respectively. This pathway leads to a molecular architecture specific to IFs and intriguing mechanical and dynamic prope...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Ulrike R ölleke Pallavi Kumari Ruth Meyer Sarah K öster Source Type: research
Lamins as structural nuclear elements through evolution
Curr Opin Cell Biol. 2023 Oct 21;85:102267. doi: 10.1016/j.ceb.2023.102267. Online ahead of print.ABSTRACTLamins are nuclear intermediate filament proteins with important, well-established roles in humans and other vertebrates. Lamins interact with DNA and numerous proteins at the nuclear envelope to determine the mechanical properties of the nucleus, coordinate chromatin organization, and modulate gene expression. Many of these functions are conserved in the lamin homologs found in basal metazoan organisms, including Drosophila and Caenorhabditis elegans. Lamin homologs have also been recently identified in non-metazoans,...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Jacob Odell Jan Lammerding Source Type: research
How do disordered head domains assist in the assembly of intermediate filaments?
Curr Opin Cell Biol. 2023 Oct 21;85:102262. doi: 10.1016/j.ceb.2023.102262. Online ahead of print.ABSTRACTThe dominant structural feature of intermediate filament (IF) proteins is a centrally located α-helix. These long α-helical segments become paired in a parallel orientation to form coiled-coil dimers. Pairs of dimers further coalesce in an anti-parallel orientation to form tetramers. These early stages of intermediate filament assembly can be accomplished solely by the central α-helices. By contrast, the assembly of tetramers into mature intermediate filaments is reliant upon an N-terminal head domain. IF head domai...
Source: Current Opinion in Cell Biology - October 23, 2023 Category: Cytology Authors: Xiaoming Zhou Masato Kato Steven L McKnight Source Type: research
