title: Regulation of neuronal survival and morphology by the E3 ubiquitin ligase RNF157.
abstract: Neuronal health is essential for the long-term integrity of the brain. In this study, we characterized the novel E3 ubiquitin ligase ring finger protein 157 (RNF157), which displays a brain-dominant expression in mouse. RNF157 is a homolog of the E3 ligase mahogunin ring finger-1, which has been previously implicated in spongiform neurodegeneration. We identified RNF157 as a regulator of survival in cultured neurons and established that the ligase activity of RNF157 is crucial for this process. We also uncovered that independently of its ligase activity, RNF157 regulates dendrite growth and maintenance. We further identified the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65) as an interactor and proteolytic substrate of RNF157 in the control of neuronal survival. Here, the nuclear localization of Fe65 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. In summary, we described that the E3 ligase RNF157 regulates important aspects of neuronal development.
authors.affiliation: Cellular and Molecular Neurobiology Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Matz
authors.affiliation: Cellular and Molecular Neurobiology Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
authors.forename: S-J
authors.initials: SJ
authors.lastname: Lee
authors.affiliation: Cellular and Molecular Neurobiology Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
authors.forename: N
authors.initials: N
authors.lastname: Schwedhelm-Domeyer
authors.affiliation: Department of Cellular Neurobiology, Schwann-Schleiden Center, Julia Lermontowa Weg 3, University of Göttingen, Göttingen, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Zanini
authors.affiliation: 1] Cellular and Molecular Neurobiology Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany [2] Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), Göttingen, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Holubowska
authors.affiliation: Cellular and Molecular Neurobiology Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Kannan
authors.affiliation: Cellular and Molecular Neurobiology Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Farnworth
authors.affiliation: 1] Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), Göttingen, Germany [2] Proteomics Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
authors.forename: O
authors.initials: O
authors.lastname: Jahn
authors.affiliation: Department of Cellular Neurobiology, Schwann-Schleiden Center, Julia Lermontowa Weg 3, University of Göttingen, Göttingen, Germany.
authors.forename: M C
authors.initials: MC
authors.lastname: Göpfert
authors.affiliation: 1] Cellular and Molecular Neurobiology Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany [2] Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), Göttingen, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Stegmüller
mesh_terms: D000818:Animals; D017209:Apoptosis; D002478:Cells, Cultured; D003712:Dendrites / Q000502:physiology; D057809:HEK293 Cells; D051548:Histone Acetyltransferases / Q000235:genetics / Q000378:metabolism; D006801:Humans; D051379:Mice; D018345:Mice, Knockout; D009419:Nerve Tissue Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism; D009474:Neurons / Q000166:cytology / Q000378:metabolism; D009687:Nuclear Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D012333:RNA, Messenger / Q000378:metabolism; D034741:RNA, Small Interfering / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D044767:Ubiquitin-Protein Ligases / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: C486243:Apbb1 protein, mouse; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D012333:RNA, Messenger; D034741:RNA, Small Interfering; D016601:RNA-Binding Proteins; D051548:Histone Acetyltransferases; C000602987:E3 ubiquitin ligase RNF157, mouse; D044767:Ubiquitin-Protein Ligases