Evolution of centrosomes and the nuclear lamina: Amoebozoan assets

Gräf, Ralph; Batsios, Petros; Meyer, Irene

doi:10.1016/j.ejcb.2015.04.004

Cited by 36 publications

(45 citation statements)

References 87 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…At least one pair of LINC core SUN-and KASH-domain proteins is found in all higher eukaryotes and, though homologs are not always readily apparent in lower eukaryotes, they have been found where a focused search has been undertaken [59]. During evolution multicellular eukaryotes have amplified both core components, but not necessarily in a linear fashion.…”

Section: Sun Trimermentioning

confidence: 99%

LINC'ing form and function at the nuclear envelope

Meinke

Schirmer²

2015

FEBS Letters

View full text Add to dashboard Cite

a b s t r a c tThe nuclear envelope is an amazing piece of engineering. On one hand it is built like a mediaeval fortress with filament systems reinforcing its membrane walls and its double membrane structure forming a lumen like a castle moat. On the other hand its structure can adapt while maintaining its integrity like a reed bending in a river. Like a fortress it has guarded drawbridges in the nuclear pore complexes, but also has other mechanical means of communication. All this is enabled largely because of the LINC complex, a multi-protein structure that connects the intermediate filament nucleoskeleton across the lumen of the double membrane nuclear envelope to multiple cytoplasmic filament systems that themselves could act simultaneously both like mediaeval buttresses and like lines on a suspension bridge. Although many details of the greater LINC structure remain to be discerned, a number of recent findings are giving clues as to how its structural organization can yield such striking dynamic yet stable properties. Combining double-and triple-helical coiled-coils, intrinsic disorder and order, tissue-specific components, and intermediate filaments enables these unique properties.

show abstract

Section: Sun Trimermentioning

confidence: 99%

LINC'ing form and function at the nuclear envelope

Meinke

Schirmer²

2015

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…Concerning cell motility, an uninterrupted series of studies in the last 50 years has led to the identification and characterization of the acto-myosin cytoskeleton underlying changes in cell shape and cell motility processes, with many cytoskeletal proteins first identified and/or characterized in Dictyostelium, such as coronin, the actin nucleator SCAR, the 34-kDa actin-crosslinking protein, myosin I and II, and formins (see Bozzaro, 2013 for references). The dynamic structure of the cell cortex, the actin cytoskeleton-nuclear membrane interactions, nucleus/nucleolus and the microtubule cytoskeleton, and their regulation by small GTPases have been the subject of several studies also in recent years (Nichols et al, 2015;Gräf et al, 2015;Rivero and Xiong, 2016;Meyer et al, 2017;Pitzen et al, 2018). Recently, the role of formins in regulating the functional integrity of the cell cortex has been investigated in detail (Junemann et al, 2016), and it has been shown that the HSBP1 protein, which regulates WASH complex assembly at centrosomes, is required for development of focal adhesion and cell polarity in Dictyostelium as well as in tumour cells (Visweshwaran et al, 2018).…”

Section: Past and Present Of A Model Organismmentioning

confidence: 99%

“…Most recent reviews or relevant papers Cytoskeleton, motility and chemotaxis Gräf et al 2015;Rivero and Xiong, 2016;Stuelten et al 2018;Liu et al 2018;van Haastert et al 2018;Edwards et al 2018;Kriebel et al 2018;Nichols et al 2019;Miyanaga et al, 2018 Phagocytosis, macropinocytosis and endo-lysosomal traffic Williams and Kay, 2018;Williams et al 2019;Pan et al 2018;Meena and Kimmel, 2017;Buckley et al, 20192019;Dunn et al 2018;Dinh et al 2018;Marinović et al, 2019 Cytokinesis Srivastava et al, 2016 Cell adhesion Fujimori et al 2019;Lampert et al 2017 Autophagy Mesquita et al 2017;Fischer et al 2019 Development, pattern formation Yamada and Schaap, 2019 Social evolution Ostrowski, 2019 Dictyostelium as model organism 325…”

Section: Biological Processmentioning

confidence: 99%

The past, present and future of Dictyostelium as a model system

Bozzaro¹

2019

Int. J. Dev. Biol.

View full text Add to dashboard Cite

The social amoeba Dictyostelium discoideum has been a preferred model organism during the last 50 years, particularly for the study of cell motility and chemotaxis, phagocytosis and macropinocytosis, intercellular adhesion, pattern formation, caspase-independent cell death and more recently autophagy and social evolution. Being a soil amoeba and professional phagocyte, thus exposed to a variety of potential pathogens, D. discoideum has also proven to be a powerful genetic and cellular model for investigating host-pathogen interactions and microbial infections. The finding that the Dictyostelium genome harbours several homologs of human genes responsible for a variety of diseases has stimulated their analysis, providing new insights into the mechanism of action of the encoded proteins and in some cases into the defect underlying the disease. Recent technological developments have covered the genetic gap between mammals and non-mammalian model organisms, challenging the modelling role of the latter. Is there a future for Dictyostelium discoideum as a model organism? Peculiarities and advantages of Dictyostelium discoideum as model organismAmong the non-mammalian model organisms, Dictyostelium discoideum (in the following Dictyostelium) is unique, due to cell division and development being totally uncoupled, and because of the transition from a unicellular to a multicellular stage during the life cycle. Growing cells proliferate by binary fission but do not differentiate, whereas starving cells undergo multicellular development and differentiation without dividing and without any need for external nutrients. Thus growth and development can be studied separately, and several non-lethal mutants can be isolated

show abstract

“…The identification of a lamin in one of the non-opisthokont branches of the eukaryotic tree of life and the improvement of bioinformatics tools facilitated identification of lamin-related protein sequences in organisms representing Archaeplastida, Excavata and SAR (Stramenopile, Alveolata, Rhizaria) (Kollmar, 2015;Preisner et al, 2018). Nowadays, there can be no doubt anymore that lamins belonged to the protein equipment of the LECA (Gräf et al, 2015;Koreny and Field, 2016).…”

Section: Historic Perspectivementioning

confidence: 99%

Nuclear envelope organization in Dictyostelium discoideum

Batsios¹,

Gräf²,

Koonce³

et al. 2019

Int. J. Dev. Biol.

Self Cite

View full text Add to dashboard Cite

The nuclear envelope consists of the outer and the inner nuclear membrane, the nuclear lamina and the nuclear pore complexes, which regulate nuclear import and export. The major constituent of the nuclear lamina of Dictyostelium is the lamin NE81. It can form filaments like B-type lamins and it interacts with Sun1, as well as with the LEM/HeH-family protein Src1. Sun1 and Src1 are nuclear envelope transmembrane proteins involved in the centrosome-nucleus connection and nuclear envelope stability at the nucleolar regions, respectively. In conjunction with a KASH-domain protein, Sun1 usually forms a so-called LINC complex. Two proteins with functions reminiscent of KASH-domain proteins at the outer nuclear membrane of Dictyostelium are known; interaptin which serves as an actin connector and the kinesin Kif9 which plays a role in the microtubule-centrosome connector. However, both of these lack the conserved KASH-domain. The link of the centrosome to the nuclear envelope is essential for the insertion of the centrosome into the nuclear envelope and the appropriate spindle formation. Moreover, centrosome insertion is involved in permeabilization of the mitotic nucleus, which ensures access of tubulin dimers and spindle assembly factors. Our recent progress in identifying key molecular players at the nuclear envelope of Dictyostelium promises further insights into the mechanisms of nuclear envelope dynamics. , and build upon the material for any purpose, even commercially), providing you give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use. Printed in Spain Abbreviations used in this paper: BAF, barrier to autointegration factor; BioID, proximity-dependent biotin identification; CDK1, cyclin-dependent kinase 1; cryo-ET, cryo-electron tomography; DAPI, 4′,6-diamidin-2-phenylindol; EM, electron microscopy; ER, endoplasmic reticulum; ExM, expansion microscopy; feSEM, field-emission scanning electron microscopy; FRAP, fluorescence recovery after photobleaching; GFP, green fluorescent protein; HeH, helix-extension-helix; IF, intermediate filament; INM, inner nuclear membrane; KASH, Klarsicht, ANC-1, Syne Homology; LBR, lamin B receptor; LECA, last eukaryotic common ancestor; LEM, lamina-associated polypeptide 2 (LAP2), Emerin, and MAN1; LINC, linker of the nucleoskeleton and the cytoskeleton; MCAK, mitotic centromere-associated kinesin; MEF, mouse embryonic fibroblast; NET, nuclear envelope transmembrane protein; NLS, nuclear localization sequence; NPC, nuclear pore complex; ONM, outer nuclear membrane; STED, stimulated emission depletion. import and export. On its nuclear side, the INM is associated with a fibrous, so-called nuclear lamina. Among the NETs, the Sun-domain proteins in the INM (e.g. Sun1) and KASH-domain proteins in the ONM (e.g. nesprin) have to be highlighted, as they form the so-called LINC complex, which spans the whole nuclear envelope (Lee and Burke, 2018...

show abstract

Evolution of centrosomes and the nuclear lamina: Amoebozoan assets

Cited by 36 publications

References 87 publications

LINC'ing form and function at the nuclear envelope

LINC'ing form and function at the nuclear envelope

The past, present and future of Dictyostelium as a model system

Nuclear envelope organization in Dictyostelium discoideum

Contact Info

Product

Resources

About