Ubiquitin-like proteins (UBLs) are a family of small proteins involved in post-translational modification of other proteins in a cell, usually with a regulatory function. The UBL protein family derives its name from the first member of the class to be discovered, ubiquitin (Ub), best known for its role in regulating protein degradation through covalent modification of other proteins. Following the discovery of ubiquitin, many additional evolutionarily related members of the group were described, involving parallel regulatory processes and similar chemistry. UBLs are involved in a widely varying array of cellular functions including autophagy, protein trafficking, inflammation and immune responses, transcription, DNA repair, RNA splicing, and cellular differentiation.
Ubiquitin itself was first discovered in the 1970s and originally named "ubiquitous immunopoietic polypeptide". Subsequently, other proteins with sequence similarity to ubiquitin were occasionally reported in the literature, but the first shown to share the key feature of covalent protein modification was ISG15, discovered in 1987. A succession of reports in the mid 1990s is recognized as a turning point in the field, with the discovery of SUMO (small ubiquitin-like modifier, also known as Sentrin or SENP1) reported around the same time by a variety of investigators in 1996, NEDD8 in 1997, and Apg12 in 1998. A systematic survey has since identified over 10,000 distinct genes for ubiquitin or ubiquitin-like proteins represented in eukaryotic genomes.
Members of the UBL family are small, non-enzymatic proteins that share a common structure exemplified by ubiquitin, which has 76 amino acid residues arranged into a "beta-grasp" protein fold consisting of a five-strand antiparallel beta sheet surrounding an alpha helix. The beta-grasp fold is widely distributed in other proteins of both eukaryotic and prokaryotic origin. Collectively, ubiquitin and ubiquitin-like proteins are sometimes referred to as "ubiquitons".
Cette page est générée automatiquement et peut contenir des informations qui ne sont pas correctes, complètes, à jour ou pertinentes par rapport à votre recherche. Il en va de même pour toutes les autres pages de ce site. Veillez à vérifier les informations auprès des sources officielles de l'EPFL.
Presentation of selected signalling pathways with emphasis on both the mechanism of action of the molecules involved, molecular interactions and the role of their spatio-temporal organization within t
Biochemistry is a key discipline for the Life Sciences. Biological Chemistry I and II are two tightly interconnected courses that aim to describe and understand in molecular terms the processes that m
L’ubiquitine ligase, ou ubiquitine ligase E3, est une ligase qui catalyse la réaction : ATP + ubiquitine + lysine–proteine AMP + diphosphate + N-ubiquityllysine–protéine. Cette enzyme recrute l' E2 chargée en ubiquitine, reconnaît une protéine substrat, et assiste ou catalyse directement le transfert de l'ubiquitine de l'enzyme E2 vers la protéine substrat. L'ubiquitine est liée à un résidu de lysine sur la protéine cible par une liaison isopeptidique.
L'ubiquitine est une protéine de 76 acides aminés servant, elle-même, de marqueur de protéines à éliminer. Elle est ainsi appelée parce qu'elle est localisée dans tous les compartiments subcellulaires de toutes les cellules des organismes, elle est dite ubiquitaire. L'ubiquitination désigne la fixation (covalente, ATP dépendante grâce à une cascade d'enzymes E1, E2, E3) spécifique et régulée d'une ou plusieurs ubiquitines sur une protéine cible (il faut quatre ubiquitines pour qu'une protéine soit dégradée).
Couvre les mécanismes d'inhibition des enzymes, les modes d'action des médicaments, la dégradation ciblée des protéines à l'aide de PROTAC, et la méthode de trou de bosse pour l'ingénierie des protéines-ligands.
DNA damage signaling following DNA double-strand breaks (DSBs) involves numerous regulating proteins, which dynamically recognize ('read') and alter ('write' or 'erase') histone post-translational modifications (PTMs). Among these PTMs, the ubiquitin syste ...
Protein ubiquitin in its +7 charge state microhydrated by 5 and 10 water molecules has been interrogated in the gas phase by cold ion UV/IR spectroscopy. The complexes were formed either by condensing water onto the unfolded bare proteins in a temperature- ...
Washington2024
, , , , , , ,
Cyclic GMP-AMP synthase (cGAS) senses aberrant DNA during infection, cancer and inflammatory disease, and initiates potent innate immune responses through the synthesis of 2 ' 3 '-cyclic GMP-AMP (cGAMP)1-7. The indiscriminate activity of cGAS towards DNA d ...