Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes

By S. Millard, S. Wood. Journal of Cell Biology, 2006

671 citations recorded by the source corpus.

Ubiquitylation is a key regulator of protein trafficking, and much about the functions of ubiquitin ligases, which add ubiquitin to substrates in this regulation, has recently come to light. However, a clear understanding of ubiquitin-dependent protein localization cannot be achieved without knowledge of the role of deubiquitylating enzymes (DUBs). DUBs, by definition, function downstream in ubiquitin pathways and, as such, have the potential to be the final editors of protein ubiquitylation status, thus determining substrate fate. This paper assimilates the current evidence concerning the substrates and activities of DUBs that regulate protein trafficking.

Subfields: Cancer Research, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/2464c212c88508f8c8a946155e6a340e9473b40b

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In Cancer Research

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In Molecular Biology

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In Oncology

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2. Walter J. Lukiw
3. D. Dormann

Citations in the corpus

• Stress-triggered phase separation is an adaptive, evolutionarily tuned response (2017, background): “…(Buchan et al., 2011; Wallace et al., 2015), certain proteins are consistently recruited, such as poly(A)binding protein (PABP; Pab1 in budding yeast) (Anderson and Kedersha, 2006), an abundant RNA-binding protein, which plays key roles in mRNA polyadenylation, stability, and translational control.”
• ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import (2010, background): “As FUS is an RNA-binding protein (Zinszner et al, 1997b), we wondered whether the observed puncta might be stress granules, cytoplasmic RNP structures that temporarily store translationally arrested mRNAs during cellular stress (Anderson and Kedersha, 2006).”
• Micro-RNA speciation in fetal, adult and Alzheimer's disease hippocampus (2007, background): “Unless mRNAs are stabilized by extrinsic factors, such as mRNAbinding proteins, antiribonuclease proteins and neutral pH, they are intrinsically unstable, rapidly degraded, information-rich molecules associated with the cytoplasmic RNA granule complex [13,14,20].”
• Cell-Free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers Within Hydrogels (2012, background): “Many of these proteins are constituents of neuronal granules, stress granules, processing bodies or polar granules (Anderson and Kedersha, 2006; Buchan and Parker, 2009; Voronina et al., 2011).”