title: Promyelocytic leukemia bodies tether to early endosomes during mitosis.
abstract: During mitosis the nuclear envelope breaks down, leading to potential interactions between cytoplasmic and nuclear components. PML bodies are nuclear structures with tumor suppressor and antiviral functions. Early endosomes, on the other hand, are cytoplasmic vesicles involved in transport and growth factor signaling. Here we demonstrate that PML bodies form stable interactions with early endosomes immediately following entry into mitosis. The 2 compartments remain stably associated throughout mitosis and dissociate in the cytoplasm of newly divided daughter cells. We also show that a minor subset of PML bodies becomes anchored to the mitotic spindle poles during cell division. The study demonstrates a stable mitosis-specific interaction between a cytoplasmic and a nuclear compartment.
authors.affiliation: Department of Microbiology and Department of Medical Biochemistry; Oslo University Hospital and University of Oslo; Oslo, Norway.
authors.forename: Vuk
authors.initials: V
authors.lastname: Palibrk
authors.affiliation: Department of Microbiology and Department of Medical Biochemistry; Oslo University Hospital and University of Oslo; Oslo, Norway.
authors.forename: Emma
authors.initials: E
authors.lastname: Lång
authors.affiliation: Department of Microbiology and Department of Medical Biochemistry; Oslo University Hospital and University of Oslo; Oslo, Norway.
authors.forename: Anna
authors.initials: A
authors.lastname: Lång
authors.affiliation: Department of Biochemistry; Institute for Cancer Research; The Norwegian Radium Hospital; Oslo University Hospital; Oslo, Norway.
authors.forename: Kay Oliver
authors.initials: KO
authors.lastname: Schink
authors.affiliation: Department of Microbiology and Department of Medical Biochemistry; Oslo University Hospital and University of Oslo; Oslo, Norway.
authors.forename: Alexander D
authors.initials: AD
authors.lastname: Rowe
authors.affiliation: Department of Microbiology and Department of Medical Biochemistry; Oslo University Hospital and University of Oslo; Oslo, Norway.
authors.forename: Stig Ove
authors.initials: SO
authors.lastname: Bøe
mesh_terms: D002460:Cell Line; D003593:Cytoplasm / Q000378:metabolism; D011992:Endosomes / Q000378:metabolism*; D006801:Humans; D045586:Intranuclear Inclusion Bodies / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D008938:Mitosis / Q000502:physiology*; D019913:Nuclear Localization Signals / Q000235:genetics; D009687:Nuclear Proteins / Q000378:metabolism*; D000071156:Promyelocytic Leukemia Protein; D020033:Protein Isoforms / Q000378:metabolism; D008941:Spindle Apparatus / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D025521:Tumor Suppressor Proteins / Q000378:metabolism*
chemical_list: D019913:Nuclear Localization Signals; D009687:Nuclear Proteins; D000071156:Promyelocytic Leukemia Protein; D020033:Protein Isoforms; D014157:Transcription Factors; D025521:Tumor Suppressor Proteins; C070576:PML protein, human
keywords: CyPNs; MAPPs; PML; PML bodies; Rab5; centrosome; endocytosis; endosomes; mitosis