Abstract
Ubiquitin-like/ubiquitin-associated proteins (UbL-UbA) are a well-studied family of non-proteasomal ubiquitin receptors that are evolutionarily conserved across species. Members of this non-homogenous family facilitate and support proteasomal activity by promoting different effects on proteostasis but exhibit diverse extra-proteasomal activities. Dysfunctional UbL-UbA proteins render cells, particularly neurons, more susceptible to stressors or aging and may cause earlier neurodegeneration. In this review, we summarized the properties and functions of UbL-UbA family members identified to date, with an emphasis on new findings obtained using Drosophila models showing a direct or indirect role in some neurodegenerative diseases.
Highlights
Protein homeostasis is a fine-tuned process that controls the biogenesis, folding, trafficking and degradation of proteins [1,2]
The intracellular elimination of toxic protein aggregates may be performed by autophagy, a process by which superfluous or potentially dangerous cytoplasmic materials are delivered to lysosomes for degradation [10]
The 26S proteasome drives incomplete degradation by a process referred to proteasomal processing that eventually releases protein fragments with new cellular functions, such as the p105 and p100 precursors of the p50 and p52 subunits of NFkB, which function in the immune system, and Gli2 and Gli3, which function in hedgehog signaling [15,16,17,18,19,20]
Summary
Protein homeostasis (proteostasis) is a fine-tuned process that controls the biogenesis, folding, trafficking and degradation of proteins [1,2]. The N-terminal UbL domain of NUB1 may bind Rpn1 and Rpn10 proteasomal subunits, while the C terminus carries two UbA domains that are involved in the interaction with ubiquitin-like proteins, as described above.
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