PMID- 31304627 OWN - NLM STAT- MEDLINE VI - 38 IP - 14 TI - Spatial and proteomic profiling reveals centrosome-independent features of centriolar satellites. PG - e101109 CI - © 2019 The Authors. Published under the terms of the CC BY NC ND 4.0 license. LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - England TA - Embo J JT - The EMBO journal JID - 8208664 IS - 1460-2075 (Electronic) LID - 10.15252/embj.2018101109 [doi] FAU - Gheiratmand, Ladan AU - Gheiratmand L AD - Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada. FAU - Coyaud, Etienne AU - Coyaud E AD - Princess Margaret Cancer Centre, University Health Network, Toronto, ON, Canada. FAU - Gupta, Gagan D AU - Gupta GD AD - Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada. FAU - Laurent, Estelle Mn AU - Laurent EM AD - Princess Margaret Cancer Centre, University Health Network, Toronto, ON, Canada. FAU - Hasegan, Monica AU - Hasegan M AD - Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada. FAU - Prosser, Suzanna L AU - Prosser SL AD - Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada. FAU - Gonçalves, João AU - Gonçalves J AD - Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada. FAU - Raught, Brian AU - Raught B AUID- ORCID: 0000-0001-6145-4776 AD - Princess Margaret Cancer Centre, University Health Network, Toronto, ON, Canada. AD - Department of Medical Biophysics, University of Toronto, Toronto, ON, Canada. FAU - Pelletier, Laurence AU - Pelletier L AUID- ORCID: 0000-0003-1171-4618 AD - Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada. AD - Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada. IS - 0261-4189 (Linking) RN - 0 (Autoantigens) RN - 0 (Cell Cycle Proteins) RN - 0 (Microtubule-Associated Proteins) RN - 0 (PCM1 protein, human) SB - IM MH - Autoantigens/*genetics/metabolism MH - Cell Cycle Proteins/*genetics/metabolism MH - Cell Line MH - Centrioles/*metabolism MH - Gene Deletion MH - Humans MH - Microtubule-Associated Proteins/metabolism MH - Protein Interaction Maps MH - Proteomics/*methods MH - Tandem Mass Spectrometry OTO - NOTNLM OT - BioID OT - centrinone OT - centriolar satellites OT - centrosome OT - proteomics PMC - PMC6627244 DCOM- 20191223 LR - 20240229 DP - 20190715 DEP - 20190603 AB - Centriolar satellites are small electron-dense granules that cluster in the vicinity of centrosomes. Satellites have been implicated in multiple critical cellular functions including centriole duplication, centrosome maturation, and ciliogenesis, but their precise composition and assembly properties have remained poorly explored. Here, we perform in vivo proximity-dependent biotin identification (BioID) on 22 human satellite proteins, to identify 2,113 high-confidence interactions among 660 unique polypeptides. Mining this network, we validate six additional satellite components. Analysis of the satellite interactome, combined with subdiffraction imaging, reveals the existence of multiple unique microscopically resolvable satellite populations that display distinct protein interaction profiles. We further show that loss of satellites in PCM1-depleted cells results in a dramatic change in the satellite interaction landscape. Finally, we demonstrate that satellite composition is largely unaffected by centriole depletion or disruption of microtubules, indicating that satellite assembly is centrosome-independent. Together, our work offers the first systematic spatial and proteomic profiling of human centriolar satellites and paves the way for future studies aimed at better understanding the biogenesis and function(s) of these enigmatic structures.