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Peptides meet ubiquitin: Simple interactions regulating complex cell signaling
Author(s) -
Veggiani Gianluca,
Sidhu Sachdev S.
Publication year - 2019
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.24091
Subject(s) - ubiquitin , proteasome , translation (biology) , peptide , biology , computational biology , protein–protein interaction , microbiology and biotechnology , biochemistry , messenger rna , gene
Abstract The interplay between the ubiquitin proteasome system (UPS) and diverse peptide motifs controls almost every aspect of cell homeostasis. To achieve such an impressive functional diversity nature has evolved hundreds of different peptide motifs that interact with proteins in the UPS and ubiquitin itself to generate an immense network of interactions. Short peptides embedded in proteins are involved in controlling the intracellular levels of proteins as well as in the translation of ubiquitin signals into biochemical events. Therefore, it is not surprising that dysregulation of such interactions is associated with many diseases, including metabolic syndromes, neurodegenerative disorders, and cancer. We review the structural and functional features of peptide motifs interacting with the UPS and their use for generating protein‐protein interaction inhibitors.