
@article {896,
	title = {Cytoskeletal control of nuclear morphology and chromatin organization.},
	journal = {J Mol Biol},
	volume = {427},
	year = {2015},
	month = {2015 Feb 13},
	pages = {695-706},
	abstract = {<p>The nucleus is sculpted toward various morphologies during cellular differentiation and development. Alterations in nuclear shape often result in changes to chromatin organization and genome function. This is thought to be reflective of its role as a cellular mechanotransducer. Recent evidence has highlighted the importance of cytoskeletal organization in defining how nuclear morphology regulates chromatin dynamics. However, the mechanisms underlying cytoskeletal control of chromatin remodeling are not well understood. We demonstrate here the differential influence of perinuclear actin- and microtubule-driven assemblies on nuclear architecture using pharmacological inhibitors and targeted RNA interference knockdown of cytoskeleton components in Drosophila cells. We find evidence that the loss of perinuclear actin assembly results in basolateral enhancement of microtubule organization and this is reflected functionally by enhanced nuclear dynamics. Cytoskeleton reorganization leads to nuclear lamina deformation that influences heterochromatin localization and core histone protein mobility. We also show that modulations in actin-microtubule assembly result in differential gene expression patterns. Taken together, we suggest that perinuclear actin and basolateral microtubule organization exerts mechanical control on nuclear morphology and chromatin dynamics.</p>
},
	keywords = {Actins, Animals, Cell Nucleus, Chromatin Assembly and Disassembly, Cytoskeleton, Drosophila melanogaster, Gene Expression Regulation, Histones, Mechanotransduction, Cellular, Nuclear Proteins},
	issn = {1089-8638},
	doi = {10.1016/j.jmb.2014.09.008},
	author = {Ramdas, Nisha M and Shivashankar, G V}
}
@article {885,
	title = {Phosphoinositide signalling in Drosophila.},
	journal = {Biochim Biophys Acta},
	volume = {1851},
	year = {2015},
	month = {2015 Jun},
	pages = {770-84},
	abstract = {<p>Phosphoinositides (PtdInsPs) are lipids that mediate a range of conserved cellular processes in eukaryotes. These include the transduction of ligand binding to cell surface receptors, vesicular transport and cytoskeletal function. The nature and functions of PtdInsPs were initially elucidated through biochemical experiments in mammalian cells. However, over the years, genetic and cell biological analysis in a range of model organisms including S. cerevisiae, D. melanogaster and C. elegans have contributed to an understanding of the involvement of PtdInsPs in these cellular events. The fruit fly Drosophila is an excellent genetic model for the analysis of cell and developmental biology as well as physiological processes, particularly analysis of the complex relationship between the cell types of a metazoan in mediating animal physiology. PtdInsP signalling pathways are underpinned by enzymes that synthesise and degrade these molecules and also by proteins that bind to these lipids in cells. In this review we provide an overview of the current understanding of PtdInsP signalling in Drosophila. We provide a comparative genomic analysis of the PtdInsP signalling toolkit between Drosophila and mammalian systems. We also review some areas of cell and developmental biology where analysis in Drosophila might provide insights into the role of this lipid-signalling pathway in metazoan biology. This article is part of a Special Issue entitled Phosphoinositides.</p>
},
	keywords = {Animals, CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase, Drosophila melanogaster, Drosophila Proteins, Gene Expression Regulation, Isoenzymes, Phosphatidylinositol 4,5-Diphosphate, Phosphoinositide Phospholipase C, Phospholipid Transfer Proteins, Receptors, Cell Surface, Signal Transduction, Species Specificity, Substrate Specificity},
	issn = {0006-3002},
	doi = {10.1016/j.bbalip.2014.10.010},
	author = {Balakrishnan, Sruthi S and Basu, Urbashi and Raghu, Padinjat}
}
