LA9 - Monoubiquitination in Endocytosis (»Add to Infobox)

Polo Simona

Simona Polo's group

Raghunath Peesari and Simona Polo IFOM, Fondazione Istituto FIRC di Oncologia Molecolare Ubiquitin (Ub) is a 76 amino acid residue protein that covalently binds to lysine residues in target proteins and regulates their stability, protein-protein interactions, sub-cellular localization and enzymatic activity. Protein ubiquitination occurs through a sequential three-step process involving ubiquitin-activating (E1), ubiquitin-conjugating (E2) and ubiquitin ligase (E3) enzymes. The addition of a single Ub moiety to a protein is known as monoubiquitination, whereas the modification of several lysine residues within a protein by single Ub moieties is known as multiple monoubiquitination. The addition of ubiquitin moieties that are themselves modified on lysine residues in an iterative fashion is known as polyubiquitination. Different types of polyubiquitination exist, depending on the particular modified lysine residue (i.e. Lys48- and Lys63-linked polyubiquitin chains) and are thought to regulate different cellular processes. Monoubiquitination is involved in regulating endocytosis of membrane proteins, DNA repair, histone activity and retroviral budding. Download the PDF file to learn how monoubiquitination is regulating endocytosis.

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Polo Simona (Principal Investigator / Simona Polo's group)

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