About: A microarray of ubiquitylated proteins for profiling deubiquitylase activity reveals the critical roles of both chain and substrate

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About: A microarray of ubiquitylated proteins for profiling deubiquitylase activity reveals the critical roles of both chain and substrate Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A microarray of ubiquitylated proteins for profiling deubiquitylase activity reveals the critical roles of both chain and substrate
Creator	Strickler, James Loch, Christian
Source	Elsevier; Medline; PMC
abstract	Abstract Substrate ubiquitylation is a reversible process critical to cellular homeostasis that is often dysregulated in many human pathologies including cancer and neurodegeneration. Elucidating the mechanistic details of this pathway could unlock a large store of information useful to the design of diagnostic and therapeutic interventions. Proteomic approaches to the questions at hand have generally utilized mass spectrometry (MS), which has been successful in identifying both ubiquitylation substrates and profiling pan-cellular chain linkages, but is generally unable to connect the two. Interacting partners of the deubiquitylating enzymes (DUBs) have also been reported by MS, although substrates of catalytically competent DUBs generally cannot be. Where they have been used towards the study of ubiquitylation, protein microarrays have usually functioned as platforms for the identification of substrates for specific E3 ubiquitin ligases. Here, we report on the first use of protein microarrays to identify substrates of DUBs, and in so doing demonstrate the first example of microarray proteomics involving multiple (i.e., distinct, sequential and opposing) enzymatic activities. This technique demonstrates the selectivity of DUBs for both substrate and type (mono- versus poly-) of ubiquitylation. This work shows that the vast majority of DUBs are monoubiquitylated in vitro, and are incapable of removing this modification from themselves. This work also underscores the critical role of utilizing both ubiquitin chains and substrates when attempting to characterize DUBs. This article is part of a Special Issue entitled: Ubiquitin Drug Discovery and Diagnostics.
has issue date	2012-11-30(xsd:dateTime)
bibo:doi	10.1016/j.bbamcr.2012.05.006
bibo:pmid	22626734
has license	els-covid
sha1sum (hex)	55bc581c140ed079689fec2fd3167aae44f063ec
schema:url	https://doi.org/10.1016/j.bbamcr.2012.05.006
resource representing a document's title	A microarray of ubiquitylated proteins for profiling deubiquitylase activity reveals the critical roles of both chain and substrate
has PubMed Central identifier	PMC7113913
has PubMed identifier	22626734
schema:publication	Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
resource representing a document's body	covid:55bc581c140ed079689fec2fd3167aae44f063ec#body_text
is schema:about of	named entity 'APPROACHES' named entity 'DISTINCT' named entity 'CELLULAR HOMEOSTASIS' named entity 'INVOLVING' named entity 'TECHNIQUE' named entity 'CELLULAR' named entity 'MAJORITY' named entity 'ACTIVITIES' named entity 'NEURODEGENERATION' named entity 'INTERACTING' named entity 'INCAPABLE' named entity 'IDENTIFYING' named entity 'WORK' named entity 'EXAMPLE' named entity 'UBIQUITYLATION' named entity 'USE OF' named entity 'THERAPEUTIC INTERVENTIONS' named entity 'INFORMATION' named entity 'HERE' named entity 'DIAGNOSTICS' named entity 'microarray' named entity 'mechanistic' named entity 'catalytically' named entity 'identify' named entity 'MICROARRAY' named entity 'REVEALS' covid:arg/55bc581c140ed079689fec2fd3167aae44f063ec named entity 'IDENTIFICATION' named entity 'MODIFICATION' named entity 'PART OF' named entity 'WHERE' named entity 'ENZYMATIC' named entity 'REMOVING' named entity 'PROTEINS' named entity 'DEUBIQUITYLASE' named entity 'CHAIN' named entity 'CHAIN' named entity 'SPECIAL' named entity 'USUALLY' named entity 'DOING' named entity 'USED' named entity 'DIAGNOSTIC' named entity 'USEFUL' named entity 'PATHWAY' named entity 'DESIGN' named entity 'HAVE' named entity '28I' named entity 'SPECIFIC' named entity 'COMPETENT' named entity 'SUBSTRATE' named entity 'MASS SPECTROMETRY' named entity 'HUMAN' named entity 'ROLES' named entity 'CRITICAL' named entity 'ISSUE' named entity 'SEQUENTIAL' named entity 'TO IDENTIFY' named entity 'CANCER' named entity 'ENZYMES' named entity 'TYPE' named entity 'REPORTED BY' named entity 'DETAILS' named entity 'PROTEIN MICROARRAYS' named entity 'CHAINS' named entity 'POLY' named entity 'REPORT' named entity 'GENERALLY' named entity 'IS A' named entity 'CRITICAL' named entity 'STORE' named entity 'TO CONNECT' named entity 'ACTIVITY' named entity 'SUBSTRATE' named entity 'PAN' named entity 'INCLUDING' named entity 'ARTICLE' named entity 'SELECTIVITY' named entity 'SUCCESSFUL' named entity 'BUT' named entity 'TO CHARACTERIZE'

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