Title :

Palmitoylation of nod1 and nod2 is required for bacterial sensing

Author(s) :

Lu, Yan [Auteur]
Zheng, Yuping [Auteur]
Coyaud, Etienne-Marie [Auteur]
Zhang, Chao [Auteur]
Selvabaskaran, Apiraam [Auteur]
Yu, Yuyun [Auteur]
Xu, Zizhen [Auteur]
Weng, Xialian [Auteur]
Chen, Ji Shun [Auteur]
Meng, Ying [Auteur]
Warner, Neil [Auteur]
Cheng, Xiawei [Auteur]
Liu, Yangyang [Auteur]
Yao, Bingpeng [Auteur]
Hu, Hu [Auteur]
Xia, Zonping [Auteur]
Muise, Aleixo M. [Auteur]
Klip, Amira [Auteur]
Brumell, John H. [Auteur]
Girardin, Stephen E. [Auteur]
Ying, Songmin [Auteur]
Fairn, Gregory D. [Auteur]
Raught, Brian [Auteur]
Sun, Qiming [Auteur]
Neculai, Dante [Auteur]

Journal title :

Science (New York, N.Y.)

Abbreviated title :

Science

Volume number :

366

Pages :

-

Publication date :

2019-10-25

ISSN :

0036-8075

HAL domain(s) :

Sciences du Vivant [q-bio]

English abstract : [en]

The nucleotide oligomerization domain (NOD)-like receptors 1 and 2 (NOD1/2) are intracellular pattern-recognition proteins that activate immune signaling pathways in response to peptidoglycans associated with microorganisms. ...
Show more >The nucleotide oligomerization domain (NOD)-like receptors 1 and 2 (NOD1/2) are intracellular pattern-recognition proteins that activate immune signaling pathways in response to peptidoglycans associated with microorganisms. Recruitment to bacteria-containing endosomes and other intracellular membranes is required for NOD1/2 signaling, and NOD1/2 mutations that disrupt membrane localization are associated with inflammatory bowel disease and other inflammatory conditions. However, little is known about this recruitment process. We found that NOD1/2 S-palmitoylation is required for membrane recruitment and immune signaling. ZDHHC5 was identified as the palmitoyltransferase responsible for this critical posttranslational modification, and several disease-associated mutations in NOD2 were found to be associated with defective S-palmitoylation. Thus, ZDHHC5-mediated S-palmitoylation of NOD1/2 is critical for their ability to respond to peptidoglycans and to mount an effective immune response.Show less >

Language :

Anglais

Audience :

Internationale

Popular science :

Non

Administrative institution(s) :

INSERM
Université de Lille

Collections :

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

Submission date :

2022-06-15T13:57:48Z