Legionella effectors SidC/SdcA ubiquitinate multiple small GTPases and SNARE proteins to promote phagosomal maturation

Protein ubiquitination is one of the most important posttranslational modifications (PTMs) in eukaryotes and is involved in the regulation of almost all cellular signaling pathways. The intracellular bacterial pathogen Legionella pneumophila translocates at least 26 effectors to hijack host ubiquiti...

Full description

Saved in:

Bibliographic Details
Published in:	Cellular and molecular life sciences : CMLS 2024-12, Vol.81 (1), p.249-249, Article 249
Main Authors:	Ma, Kelong, Shu, Rundong, Liu, Hongtao, Ge, Jinli, Liu, Jiayang, Lu, Qian, Fu, Jiaqi, Liu, Xiaoyun, Qiu, Jiazhang
Format:	Article
Language:	English
Subjects:	Animals Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry Biomedical and Life Sciences Biomedicine Cell Biology Effectors Endoplasmic reticulum Endoplasmic Reticulum - metabolism Eukaryotes eukaryotic cells guanosinetriphosphatase HEK293 Cells Humans Intracellular signalling Legionella Legionella pneumophila Legionella pneumophila - metabolism Legionnaires' disease bacterium Life Sciences Lysosomal protein Lysosomes Maturation Membrane fusion Membrane vesicles Membranes Mice Monomeric GTP-Binding Proteins - metabolism N-Ethylmaleimide N-Ethylmaleimide-sensitive protein Original Original Article pathogens phagosomes Phagosomes - metabolism Phagosomes - microbiology Proteins Qa-SNARE Proteins - metabolism rab GTP-Binding Proteins - metabolism rab7 GTP-Binding Proteins - metabolism Signal transduction SNAP receptors SNARE Proteins - metabolism Substrates Syntaxin Syntaxin 4 Ubiquitin ubiquitin-protein ligase Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination vacuoles Vacuoles - metabolism Vacuoles - microbiology Vesicle fusion Vesicles
Citations:	Items that this one cites Items that cite this one
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!