@article{12421, abstract = {The actin cytoskeleton plays a key role in cell migration and cellular morphodynamics in most eukaryotes. The ability of the actin cytoskeleton to assemble and disassemble in a spatiotemporally controlled manner allows it to form higher-order structures, which can generate forces required for a cell to explore and navigate through its environment. It is regulated not only via a complex synergistic and competitive interplay between actin-binding proteins (ABP), but also by filament biochemistry and filament geometry. The lack of structural insights into how geometry and ABPs regulate the actin cytoskeleton limits our understanding of the molecular mechanisms that define actin cytoskeleton remodeling and, in turn, impact emerging cell migration characteristics. With the advent of cryo-electron microscopy (cryo-EM) and advanced computational methods, it is now possible to define these molecular mechanisms involving actin and its interactors at both atomic and ultra-structural levels in vitro and in cellulo. In this review, we will provide an overview of the available cryo-EM methods, applicable to further our understanding of the actin cytoskeleton, specifically in the context of cell migration. We will discuss how these methods have been employed to elucidate ABP- and geometry-defined regulatory mechanisms in initiating, maintaining, and disassembling cellular actin networks in migratory protrusions.}, author = {Fäßler, Florian and Javoor, Manjunath and Schur, Florian KM}, issn = {1470-8752}, journal = {Biochemical Society Transactions}, keywords = {Biochemistry}, number = {1}, pages = {87--99}, publisher = {Portland Press}, title = {{Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM}}, doi = {10.1042/bst20220221}, volume = {51}, year = {2023}, } @article{1915, abstract = {ROPs (Rho of plants) belong to a large family of plant-specific Rho-like small GTPases that function as essential molecular switches to control diverse cellular processes including cytoskeleton organization, cell polarization, cytokinesis, cell differentiation and vesicle trafficking. Although the machineries of vesicle trafficking and cell polarity in plants have been individually well addressed, how ROPs co-ordinate those processes is still largely unclear. Recent progress has been made towards an understanding of the coordination of ROP signalling and trafficking of PIN (PINFORMED) transporters for the plant hormone auxin in both root and leaf pavement cells. PIN transporters constantly shuttle between the endosomal compartments and the polar plasma membrane domains, therefore the modulation of PIN-dependent auxin transport between cells is a main developmental output of ROP-regulated vesicle trafficking. The present review focuses on these cellular mechanisms, especially the integration of ROP-based vesicle trafficking and plant cell polarity.}, author = {Chen, Xu and Friml, Jirí}, issn = {1470-8752}, journal = {Biochemical Society Transactions}, number = {1}, pages = {212 -- 218}, publisher = {Portland Press}, title = {{Rho-GTPase-regulated vesicle trafficking in plant cell polarity}}, doi = {10.1042/BST20130269}, volume = {42}, year = {2014}, } @article{12200, abstract = {Key steps in the evolution of the angiosperm anther include the patterning of the concentrically organized microsporangium and the incorporation of four such microsporangia into a leaf-like structure. Mutant studies in the model plant Arabidopsis thaliana are leading to an increasingly accurate picture of (i) the cell lineages culminating in the different cell types present in the microsporangium (the microsporocytes, the tapetum, and the middle and endothecial layers), and (ii) some of the genes responsible for specifying their fates. However, the processes that confer polarity on the developing anther and position the microsporangia within it remain unclear. Certainly, data from a range of experimental strategies suggest that hormones play a central role in establishing polarity and the patterning of the anther initial, and may be responsible for locating the microsporangia. But the fact that microsporangia were originally positioned externally suggests that their development is likely to be autonomous, perhaps with the reproductive cells generating signals controlling the growth and division of the investing anther epidermis. These possibilities are discussed in the context of the expression of genes which initiate and maintain male and female reproductive development, and in the perspective of our current views of anther evolution.}, author = {Feng, Xiaoqi and Dickinson, Hugh G.}, issn = {0300-5127}, journal = {Biochemical Society Transactions}, keywords = {Biochemistry, Anther Development, Arabidopsis, Cell Fate, Microsporangium, Polarity, Receptor Kinase}, number = {2}, pages = {571--576}, publisher = {Portland Press Ltd.}, title = {{Cell–cell interactions during patterning of the Arabidopsis anther}}, doi = {10.1042/bst0380571}, volume = {38}, year = {2010}, } @article{1951, author = {Sazanov, Leonid A and Burrows, Paul and Nixon, Peter}, issn = {0300-5127}, journal = {Biochemical Society Transactions}, number = {3}, pages = {739 -- 743}, publisher = {Portland Press}, title = {{Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids}}, doi = {10.1042/bst0240739}, volume = {24}, year = {1996}, } @article{1948, author = {Sazanov, Leonid A and Jackson, Julie}, issn = {0300-5127}, journal = {Biochemical Society Transactions}, number = {3}, pages = {260}, publisher = {Portland Press}, title = {{Possible functions of the NADP-linked isocitrate dehydrogenase and H+ -transhydrogenase in heart mitochondria }}, doi = {10.1042/bst021260s}, volume = {21}, year = {1993}, } @article{1950, author = {Jackson, Julie and Cotton, N P J and Williams, Ross and Bizouarn, Tania and Hutton, Mike and Sazanov, Leonid A and Thomas, Christopher}, issn = {0300-5127}, journal = {Biochemical Society Transactions}, number = {4}, pages = {1010 -- 1013}, publisher = {Portland Press}, title = {{Proton-translocating transhydrogenase in bacteria}}, doi = {10.1042/bst0211010}, volume = {21}, year = {1993}, }