TY - JOUR
T1 - Diverse ubiquitin codes in the regulation of inflammatory signaling
AU - Ikeda, Fumiyo
AU - Shigekazu Nagata, M. J.A.
N1 - Funding Information:
Fumiyo Ikeda (born and raised in Osaka, Japan) graduated from the Dental School of Osaka University in 1999. She obtained a PhD degree from Osaka University in 2003 on the discovery of the transcription factor NFAT1 as a critical lineage determination factor during osteoclastogenesis. She continued as a postdoctoral fellow (supported by the Uehara Foundation, the Humboldt Foundation, and JSPS) in the Ivan Dikic lab at Goethe University (Frankfurt, Germany) where she studied a link between inflammatory responses and the ubiquitin system. During this period (2005–2011), she made a major contribution to the ubiquitin research field by the discovery of a new function of a novel type of ubiquitin chain in inflammatory cellular signaling. She served as an independent group leader at the Institute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA, Vienna, Austria) from 2011 to 2019, and moved to the Medical Institute of Bioregulation (MIB), Kyushu University, as a professor. Her team aims to understand how the ubiquitin system regulates inflammatory responses using various approaches, including biochemical, molecular, and cellular techniques as well as animal models. For her past achievements, she received the Dr. Paul und Cilli Weill Foundation Award in 2010 (Germany) and the JSPS Prize in 2019 (Japan).
Funding Information:
Research in the Ikeda lab is supported by JSPS KAKENHI Grant Number JP18K19959. I acknowledge all Ikeda lab members past and present.
PY - 2020
Y1 - 2020
N2 - Ubiquitin is a small protein used for posttranslational modification and it regulates every aspect of biological functions. Through a three-step cascade of enzymatic action, ubiquitin is conjugated to a substrate. Because ubiquitin itself can be post-translationally modified, this small protein generates various ubiquitin codes and triggers differing regulation of biological functions. For example, ubiquitin itself can be ubiquitinated, phosphorylated, acetylated, or SUMOylated. Via the type three secretion system, some bacterial effectors also modify the ubiquitin system in host cells. This review describes the general concept of the ubiquitin system as well as the fundamental functions of ubiquitin in the regulation of cellular responses during inflammation and bacterial infection.
AB - Ubiquitin is a small protein used for posttranslational modification and it regulates every aspect of biological functions. Through a three-step cascade of enzymatic action, ubiquitin is conjugated to a substrate. Because ubiquitin itself can be post-translationally modified, this small protein generates various ubiquitin codes and triggers differing regulation of biological functions. For example, ubiquitin itself can be ubiquitinated, phosphorylated, acetylated, or SUMOylated. Via the type three secretion system, some bacterial effectors also modify the ubiquitin system in host cells. This review describes the general concept of the ubiquitin system as well as the fundamental functions of ubiquitin in the regulation of cellular responses during inflammation and bacterial infection.
UR - http://www.scopus.com/inward/record.url?scp=85096081666&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85096081666&partnerID=8YFLogxK
U2 - 10.2183/pjab.96.032
DO - 10.2183/pjab.96.032
M3 - Review article
C2 - 33177297
AN - SCOPUS:85096081666
SN - 0386-2208
VL - 96
SP - 431
EP - 439
JO - Proceedings of the Japan Academy Series B: Physical and Biological Sciences
JF - Proceedings of the Japan Academy Series B: Physical and Biological Sciences
IS - 9
ER -