TY - JOUR
T1 - Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin
AU - Fujita, Naonobu
AU - Morita, Eiji
AU - Itoh, Takashi
AU - Tanaka, Atsushi
AU - Nakaoka, Megumi
AU - Osada, Yuki
AU - Umemoto, Tetsuo
AU - Saitoh, Tatsuya
AU - Nakatogawa, Hitoshi
AU - Kobayashi, Shouhei
AU - Haraguchi, Tokuko
AU - Guan, Jun Lin
AU - Iwai, Kazuhiro
AU - Tokunaga, Fuminori
AU - Saito, Kazunobu
AU - Ishibashi, Koutaro
AU - Akira, Shizuo
AU - Fukuda, Mitsunori
AU - Noda, Takeshi
AU - Yoshimori, Tamotsu
PY - 2013
Y1 - 2013
N2 - Although ubiquitin is thought to be important for the autophagic sequestration of invading bacteria (also called xenophagy), its precise role remains largely enigmatic. Here we determined how ubiquitin is involved in this process. After invasion, ubiquitin is conjugated to host cellular proteins in endosomes that contain Salmonella or transfection reagent-coated latex (polystyrene) beads, which mimic invading bacteria. Ubiquitin is recognized by the autophagic machinery independently of the LC3-ubiquitin interaction through adaptor proteins, including a direct interaction between ubiquitin and Atg16L1. To ensure that invading pathogens are captured and degraded, Atg16L1 targeting is secured by two backup systems that anchor Atg16L1 to ubiquitin-decorated endosomes. Thus, we reveal that ubiquitin is a pivotal molecule that connects bacteriacontaining endosomes with the autophagic machinery upstream of LC3.
AB - Although ubiquitin is thought to be important for the autophagic sequestration of invading bacteria (also called xenophagy), its precise role remains largely enigmatic. Here we determined how ubiquitin is involved in this process. After invasion, ubiquitin is conjugated to host cellular proteins in endosomes that contain Salmonella or transfection reagent-coated latex (polystyrene) beads, which mimic invading bacteria. Ubiquitin is recognized by the autophagic machinery independently of the LC3-ubiquitin interaction through adaptor proteins, including a direct interaction between ubiquitin and Atg16L1. To ensure that invading pathogens are captured and degraded, Atg16L1 targeting is secured by two backup systems that anchor Atg16L1 to ubiquitin-decorated endosomes. Thus, we reveal that ubiquitin is a pivotal molecule that connects bacteriacontaining endosomes with the autophagic machinery upstream of LC3.
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U2 - 10.1083/jcb.201304188
DO - 10.1083/jcb.201304188
M3 - Article
C2 - 24100292
AN - SCOPUS:84886897936
VL - 203
SP - 115
EP - 128
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 1
ER -