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Expansion of DUB functionality generated by alternative isoforms - USP35, a case study.

Pawel Leznicki1, Jayaprakash Natarajan2, Gerd Bader3

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Journal of Cell Science
|April 25, 2018
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Summary
This summary is machine-generated.

Deubiquitylating enzymes (DUBs) regulate protein ubiquitylation. This study reveals alternative USP35 isoforms with distinct cellular roles, expanding DUB functional diversity and impacting apoptosis and ER stress.

Keywords:
ApoptosisDeubiquitinaseEndoplasmic reticulumLipid dropletsUbiquitin signalling

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Protein ubiquitylation is a reversible post-translational modification crucial for cellular processes.
  • Deubiquitylating enzymes (DUBs) reverse ubiquitylation, but their limited number (around 100) poses a challenge in explaining the regulation of thousands of ubiquitylation events.
  • The functional expansion of DUBs remains an area of active investigation.

Purpose of the Study:

  • To investigate how the limited number of DUBs in mammalian cells can regulate numerous ubiquitylation events.
  • To explore the role of alternative splicing and isoforms in expanding DUB functional diversity.
  • To characterize the specific functions of different USP35 isoforms.

Main Methods:

  • Analysis of annotated human DUB transcripts to identify novel DUB-coding transcripts.
  • Case study using USP35, a less-studied DUB, to investigate alternative isoforms.
  • Experimental manipulation of USP35 isoform levels and localization studies.
  • Assessment of apoptosis induction by staurosporine and TNF-related apoptosis-inducing ligand (TRAIL).
  • Analysis of endoplasmic reticulum (ER) stress and lipid homeostasis.

Main Results:

  • Identification of approximately 300 additional ribosome-associated, protein-coding DUB transcripts, increasing the known DUB repertoire.
  • Discovery of two distinct USP35 isoforms with differential subcellular localization and functions.
  • USP35 isoform 1 acts as an anti-apoptotic factor, inhibiting TRAIL-induced apoptosis.
  • USP35 isoform 2, localized to the ER and lipid droplets, induces ER stress and cell death upon manipulation, likely via lipid homeostasis deregulation.

Conclusions:

  • Alternative splicing leading to distinct DUB isoforms is a key mechanism for functional expansion within the DUB family.
  • USP35 isoforms exhibit opposing roles in cell fate, regulating apoptosis and ER stress.
  • This study provides a new perspective on DUB regulation and function, highlighting the importance of isoform diversity.