Titre :

Fam105a/otulinl is a pseudodeubiquitinase of the otu-class that localizes to the er membrane

Auteur(s) :

Ceccarelli, Derek F. [Auteur]
Ivantsiv, Sofiia [Auteur]
Mullin, Amber Anne [Auteur]
Coyaud, Etienne-Marie [Auteur]
Manczyk, Noah [Auteur]
Maisonneuve, Pierre [Auteur]
Kurinov, Igor [Auteur]
Zhao, Liang [Auteur]
Go, Chris [Auteur]
Gingras, Anne-Claude [Auteur]
Raught, Brian [Auteur]
Cordes, Sabine [Auteur]
Sicheri, Frank [Auteur]

Titre de la revue :

Structure (London, England . 1993)

Nom court de la revue :

Structure

Numéro :

27

Pagination :

-

Date de publication :

2019-06-04

ISSN :

0969-2126

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

Pseudoenzymes have been identified across a diverse range of enzyme classes and fulfill important cellular functions. Examples of pseudoenzymes exist within ubiquitin conjugating and deubiquitinase (DUB) protein families. ...
Lire la suite >Pseudoenzymes have been identified across a diverse range of enzyme classes and fulfill important cellular functions. Examples of pseudoenzymes exist within ubiquitin conjugating and deubiquitinase (DUB) protein families. Here we characterize FAM105A/OTULINL, the only putative pseudodeubiquitinase of the ovarian tumor protease (OTU domain) family in humans. The crystal structure of FAM105A revealed that the OTU domain possesses structural deficiencies in both active site and substrate-binding infrastructure predicted to impair normal DUB function. We confirmed the absence of catalytic function against all ubiquitin linkages and an inability of FAM105A to bind ubiquitin compared with catalytically active FAM105B/OTULIN. FAM105A co-localized with KDEL markers and Lamin B1 at the endoplasmic reticulum (ER) and nuclear envelope, respectively. Accordingly, the FAM105A interactome exhibited significant enrichment in proteins localized to the ER/outer nuclear, Golgi and vesicular membranes. In light of undetectable deubiquitinase activity, we posit that FAM105A/OTULINL functions through its ability to mediate protein-protein interactions.Lire moins >

Langue :

Anglais

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

INSERM
Université de Lille

Collections :

• Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192

Date de dépôt :

2022-06-15T13:57:42Z