Lymphocyte-specific murine deubiquitinating enzymes induced by cytokines.
It is becoming clear that a number of proteins regulating cellular mechanisms for homeostasis in all eukaryotes are controlled not only by phosphorylation and dephosphorylation but also by ubiquitination and deubiquitination. This includes most of oncoproteins and signaling components involved in receptor tyrosine kinase (RTK)-mediated signal transduction pathways. Like protein phosphorylation and dephosphorylation regulated by kinases and phosphatases, respectively, protein ubiquitination and deubiquitination are very dynamic and are regulated by ubiquitin conjugating enzymes and deubiquitinating (DUB) enzymes. A number of deubiquitinating enzymes have been isolated even though little is known about their biological functions. This review concentrates on recent findings and new insights into DUB enzyme subfamily members in lymphocytes.
Baek
Kwang-Hyun
KH
Department of Microbiology, College of Medicine, Pochon CHA University, Cell and Gene Therapy Research Institute, CHA General Hospital, Kangnam-Gu, Seoul, Korea. baek@cha.ac.kr
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D003546:Cysteine Endopeptidases / Q000378:metabolism; D016207:Cytokines / Q000494:pharmacology*; D010450:Endopeptidases / Q000096:biosynthesis* / Q000737:chemistry; D004790:Enzyme Induction / Q000187:drug effects; D006801:Humans; D017874:Immediate-Early Proteins / Q000096:biosynthesis* / Q000737:chemistry; D008214:Lymphocytes / Q000187:drug effects / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D016207:Cytokines; D017874:Immediate-Early Proteins; D009097:Multienzyme Complexes; C099271:Dub1 protein, mouse; C103857:Dub2 protein, mouse; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex