The ACS Virgo Cluster Survey. VIII. The Nuclei of Early-Type Galaxies

(Abridged) The ACS Virgo Cluster Survey is an HST program to obtain high-resolution, g and z-band images for 100 early-type members of the Virgo Cluster, spanning a range of ~460 in blue luminosity. Based on this large, homogeneous dataset, we present a sharp upward revision in the frequency of nucleation in early-type galaxies brighter than M_B ~ -15 (66 < f_n < 82%), and find no evidence for nucleated dwarfs to be more concentrated to the center of Virgo than their non-nucleated counterparts. Resolved stellar nuclei are not present in galaxies brighter than M_B ~ -20.5, however, there is no clear evidence from the properties of the nuclei, or from the overall incidence of nucleation, for a change at M_B ~ -17.6, the traditional dividing point between dwarf and giant galaxies. On average, nuclei are ~3.5 mag brighter than a typical globular cluster and have a median half-light radius ~4.2 pc. Nuclear luminosities correlate with nuclear sizes and, in galaxies fainter than M_B ~ -17.6, nuclear colors. Comparing the nuclei to the "nuclear clusters" found in late-type spiral galaxies reveals a close match in terms of size, luminosity and overall frequency, pointing to a formation mechanism that is rather insensitive to the detailed properties of the host galaxy. The mean nuclear-to-galaxy luminosity ratio is indistinguishable from the mean SBH-to-bulge mass ratio, calculated in early-type galaxies with detected supermassive black holes (SBHs). We argue that compact stellar nuclei might be the low-mass counterparts of the SBHs detected in the bright galaxies, and that one should think in terms of "Central Massive Objects" -- either SBHs or compact stellar nuclei -- that accompany the formation of almost all early-type galaxies and contain a mean fraction ~0.3% of the total bulge mass.Comment: ApJ Supplements, accepted. Updated references. The manuscript is 61 pages, including 6 tables and 28 figures. Figures included in this submission are low resolution; a version of the paper containing high-resolution color figures can be downloaded from the ACSVCS website: http://www.cadc.hia.nrc.gc.ca/community/ACSVCS/publications.html#acsvcs

Faint stellar systems in the Virgo cluster: ultracompact dwarfs and globular clusters

We examine the properties of ten compact objects in the vicinity of M87 using HST imaging and Keck spectroscopy. We find three objects to be larger and brighter than typical globular clusters; they resemble the nuclei of nucleated dEs in Virgo, having similar massto-light ratios, luminosities and colors. Their properties are consistent with models of tidally stripping of nucleated dEs. One object could be an old \u201cstellar supercluster\u201d, formed through the amalgamation of multiple young massive clusters. Two other objects appear to be massive versions of otherwise \u201cnormal\u201d globular clusters.Peer reviewed: YesNRC publication: Ye

Table S2 from CEP19 cooperates with FOP and CEP350 to drive early steps in the ciliogenesis programme

Primary cilia are microtubule-based sensory organelles necessary for efficient transduction of extracellular cues. To initiate cilia formation, ciliary vesicles (CVs) are transported to the vicinity of the centrosome where they dock to the distal end of the mother centriole and fuse to initiate cilium assembly. However, to this date, the early steps in cilia formation remain incompletely understood. Here, we demonstrate functional interplay between CEP19, FOP and CEP350 in ciliogenesis. Using three-dimensional structured-illumination microscopy (3D-SIM) imaging, we mapped the relative spatial distribution of these proteins at the distal end of the mother centriole and show that CEP350/FOP act upstream of CEP19 in their recruitment hierarchy. We demonstrate that CEP19 CRISPR KO cells are severely impaired in their ability to form cilia, analogous to the loss of function of CEP19 binding partners FOP and CEP350. Using GFP-tagged deletion constructs of CEP19, we show that the C-terminus of CEP19 is required for both its localization to centrioles and for its function in ciliogenesis. Critically, this region also mediates the interaction between CEP19 and FOP/CEP350. Interestingly, a morbid obesity-associated R82* truncated mutant of CEP19 cannot ciliate nor interact with FOP and CEP350, indicative of a putative role for CEP19 in ciliopathies. Finally, analysis of CEP19 KO cells using thin-section electron microscopy revealed marked defects in the docking of CVs to the distal end of the mother centrioles. Together, these data demonstrate a role for the CEP19, FOP and CEP350 module in ciliogenesis and the possible effect of disrupting their functions in ciliopathies

Figure S1 from CEP19 cooperates with FOP and CEP350 to drive early steps in the ciliogenesis programme

Primary cilia are microtubule-based sensory organelles necessary for efficient transduction of extracellular cues. To initiate cilia formation, ciliary vesicles (CVs) are transported to the vicinity of the centrosome where they dock to the distal end of the mother centriole and fuse to initiate cilium assembly. However, to this date, the early steps in cilia formation remain incompletely understood. Here, we demonstrate functional interplay between CEP19, FOP and CEP350 in ciliogenesis. Using three-dimensional structured-illumination microscopy (3D-SIM) imaging, we mapped the relative spatial distribution of these proteins at the distal end of the mother centriole and show that CEP350/FOP act upstream of CEP19 in their recruitment hierarchy. We demonstrate that CEP19 CRISPR KO cells are severely impaired in their ability to form cilia, analogous to the loss of function of CEP19 binding partners FOP and CEP350. Using GFP-tagged deletion constructs of CEP19, we show that the C-terminus of CEP19 is required for both its localization to centrioles and for its function in ciliogenesis. Critically, this region also mediates the interaction between CEP19 and FOP/CEP350. Interestingly, a morbid obesity-associated R82* truncated mutant of CEP19 cannot ciliate nor interact with FOP and CEP350, indicative of a putative role for CEP19 in ciliopathies. Finally, analysis of CEP19 KO cells using thin-section electron microscopy revealed marked defects in the docking of CVs to the distal end of the mother centrioles. Together, these data demonstrate a role for the CEP19, FOP and CEP350 module in ciliogenesis and the possible effect of disrupting their functions in ciliopathies

Figure S2 from CEP19 cooperates with FOP and CEP350 to drive early steps in the ciliogenesis programme

Primary cilia are microtubule-based sensory organelles necessary for efficient transduction of extracellular cues. To initiate cilia formation, ciliary vesicles (CVs) are transported to the vicinity of the centrosome where they dock to the distal end of the mother centriole and fuse to initiate cilium assembly. However, to this date, the early steps in cilia formation remain incompletely understood. Here, we demonstrate functional interplay between CEP19, FOP and CEP350 in ciliogenesis. Using three-dimensional structured-illumination microscopy (3D-SIM) imaging, we mapped the relative spatial distribution of these proteins at the distal end of the mother centriole and show that CEP350/FOP act upstream of CEP19 in their recruitment hierarchy. We demonstrate that CEP19 CRISPR KO cells are severely impaired in their ability to form cilia, analogous to the loss of function of CEP19 binding partners FOP and CEP350. Using GFP-tagged deletion constructs of CEP19, we show that the C-terminus of CEP19 is required for both its localization to centrioles and for its function in ciliogenesis. Critically, this region also mediates the interaction between CEP19 and FOP/CEP350. Interestingly, a morbid obesity-associated R82* truncated mutant of CEP19 cannot ciliate nor interact with FOP and CEP350, indicative of a putative role for CEP19 in ciliopathies. Finally, analysis of CEP19 KO cells using thin-section electron microscopy revealed marked defects in the docking of CVs to the distal end of the mother centrioles. Together, these data demonstrate a role for the CEP19, FOP and CEP350 module in ciliogenesis and the possible effect of disrupting their functions in ciliopathies

Figure S4 from CEP19 cooperates with FOP and CEP350 to drive early steps in the ciliogenesis programme

Primary cilia are microtubule-based sensory organelles necessary for efficient transduction of extracellular cues. To initiate cilia formation, ciliary vesicles (CVs) are transported to the vicinity of the centrosome where they dock to the distal end of the mother centriole and fuse to initiate cilium assembly. However, to this date, the early steps in cilia formation remain incompletely understood. Here, we demonstrate functional interplay between CEP19, FOP and CEP350 in ciliogenesis. Using three-dimensional structured-illumination microscopy (3D-SIM) imaging, we mapped the relative spatial distribution of these proteins at the distal end of the mother centriole and show that CEP350/FOP act upstream of CEP19 in their recruitment hierarchy. We demonstrate that CEP19 CRISPR KO cells are severely impaired in their ability to form cilia, analogous to the loss of function of CEP19 binding partners FOP and CEP350. Using GFP-tagged deletion constructs of CEP19, we show that the C-terminus of CEP19 is required for both its localization to centrioles and for its function in ciliogenesis. Critically, this region also mediates the interaction between CEP19 and FOP/CEP350. Interestingly, a morbid obesity-associated R82* truncated mutant of CEP19 cannot ciliate nor interact with FOP and CEP350, indicative of a putative role for CEP19 in ciliopathies. Finally, analysis of CEP19 KO cells using thin-section electron microscopy revealed marked defects in the docking of CVs to the distal end of the mother centrioles. Together, these data demonstrate a role for the CEP19, FOP and CEP350 module in ciliogenesis and the possible effect of disrupting their functions in ciliopathies