Characterizing polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB+1

Michal Chojnacki, Daoning Zhang, Monika Talarowska, Piotr Gałecki, Janusz Szemraj, David Fushman, Mark A Nakasone (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


The ubiquitin mutant UBB+1 has been identified as a hallmark of neurodegenerative diseases. In this study, we characterize polyubiquitinated forms of UBB+1 in vitro and from patient samples. The ability of UBB+1 to be readily ubiquitinated by several E2 enzymes provided a mechanism for the controlled synthesis and purification of defined conjugates. This allowed us to utilize polyUb-UBB+1 conjugates for biochemical assays, as well as solution NMR. Coupled with our immunoassay for detection of ubiquitinated forms of UBB+1 in patient blood samples, we gain a clearer picture of the molecular mechanisms underlying neurodegenerative diseases.

Original languageEnglish
Pages (from-to)4573-4585
Number of pages13
JournalFEBS Letters
Issue number24
Early online date22 Nov 2016
Publication statusPublished - 23 Dec 2016


  • Aged
  • Alzheimer Disease/genetics
  • Case-Control Studies
  • Cysteine Endopeptidases/chemistry
  • Deubiquitinating Enzymes
  • Endopeptidases/chemistry
  • Endosomal Sorting Complexes Required for Transport/chemistry
  • Female
  • Fluoresceins/chemistry
  • Fluorescent Dyes/chemistry
  • Gene Expression Regulation
  • Humans
  • Male
  • Middle Aged
  • Models, Molecular
  • Neurons/metabolism
  • Nuclear Magnetic Resonance, Biomolecular
  • Polyubiquitin/chemistry
  • Proteasome Endopeptidase Complex/metabolism
  • Protein Isoforms/chemistry
  • Protein Structure, Secondary
  • Staining and Labeling
  • Ubiquitin/chemistry
  • Ubiquitin Thiolesterase/chemistry
  • Ubiquitin-Specific Proteases/chemistry
  • Ubiquitination


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