The Centrosome Neither Persistently Leads Migration nor Determines the Site of Axonogenesis in Migrating Neurons in Vivo Jcb: Correction Jcb: Article
نویسندگان
چکیده
Figure 1. Identification of subcellular markers for in vivo imaging of zebrafish cells. Images of zebrafish Pac2 fibroblasts transfected with pCS2+ constructs encoding fluorescently tagged markers for subcellular labeling 24 h after transfection. (A) b3-Tubulin-GFP, (B) GFP-tubulin, (C) EB1-GFP, (D) GFP-DCX, (E) Tau-GFP, and (F) EB3-GFP. (G) mito-DsRed to label mitochondria in red, YFP-DCX to label microtubules in yellow, memCFP to label the cytoplasmic membrane in blue and H2B-CFP to label the nucleus in blue; (H) DsRed2-ER to label the ER in red, Golgi-Citrine to label the Golgi apparatus in yellow, memCFP and H2B-CFP; (I) DCX-tdTomato to label microtubules in red, Citrine-Actin to label the actin cytoskeleton in yellow, memCFP, H2B-CFP; (J) Centrin2-YFP to label the centrosome in yellow (arrow is indicating the two centrioles of the centrosome) and H2B-CFP; (K) GFP-Centrin2 to label the centrosome in green (arrow is indicating the two centrioles of the centrosome); and (L) DCX-tdTomato, Centrin2-YFP, memCFP, and H2B-CFP. The inset shows a higher magnification of the centrosome at the hub of the microtubule network. These data present a collection of subcellular-targeted fluorescent proteins tested for their specificity in zebrafish cells. " mem " represents a membrane localization signal, which consists of a palmitylation and myristinylation sequence of the human Lck kinase.
منابع مشابه
The centrosome neither persistently leads migration nor determines the site of axonogenesis in migrating neurons in vivo
The position of the centrosome ahead of the nucleus has been considered crucial for coordinating neuronal migration in most developmental situations. The proximity of the centrosome has also been correlated with the site of axonogenesis in certain differentiating neurons. Despite these positive correlations, accumulating experimental findings appear to negate a universal role of the centrosome ...
متن کاملSliding of centrosome-unattached microtubules defines key features of neuronal phenotype
Contemporary models for neuronal migration are grounded in the view that virtually all functionally relevant microtubules (MTs) in migrating neurons are attached to the centrosome, which occupies a position between the nucleus and a short leading process. It is assumed that MTs do not undergo independent movements but rather transduce forces that enable movements of the centrosome and nucleus. ...
متن کاملERK regulates Golgi and centrosome orientation towards the leading edge through GRASP65
Directed cell migration requires the orientation of the Golgi and centrosome toward the leading edge. We show that stimulation of interphase cells with the mitogens epidermal growth factor or lysophosphatidic acid activates the extracellular signal-regulated kinase (ERK), which phosphorylates the Golgi structural protein GRASP65 at serine 277. Expression of a GRASP65 Ser277 to alanine mutant or...
متن کاملOne-dimensional topography underlies three-dimensional fibrillar cell migration
Current concepts of cell migration were established in regular two-dimensional (2D) cell culture, but the roles of topography are poorly understood for cells migrating in an oriented 3D fibrillar extracellular matrix (ECM). We use a novel micropatterning technique termed microphotopatterning (microPP) to identify functions for 1D fibrillar patterns in 3D cell migration. In striking contrast to ...
متن کاملMutation of the α-tubulin Tuba1a leads to straighter microtubules and perturbs neuronal migration
Brain development involves extensive migration of neurons. Microtubules (MTs) are key cellular effectors of neuronal displacement that are assembled from α/β-tubulin heterodimers. Mutation of the α-tubulin isotype TUBA1A is associated with cortical malformations in humans. In this study, we provide detailed in vivo and in vitro analyses of Tuba1a mutants. In mice carrying a Tuba1a missense muta...
متن کامل