Lymphocyte-specific murine deubiquitinating enzymes induced by cytokines

Am J Hematol. 2002 Dec;71(4):340-5. doi: 10.1002/ajh.10243.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Conserved Sequence
  • Cysteine Endopeptidases / metabolism
  • Cytokines / pharmacology*
  • Endopeptidases / biosynthesis*
  • Endopeptidases / chemistry
  • Enzyme Induction / drug effects
  • Humans
  • Immediate-Early Proteins / biosynthesis*
  • Immediate-Early Proteins / chemistry
  • Lymphocytes / drug effects
  • Lymphocytes / enzymology*
  • Mice
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism
  • Proteasome Endopeptidase Complex
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Cytokines
  • Immediate-Early Proteins
  • Multienzyme Complexes
  • Dub1 protein, mouse
  • Dub2 protein, mouse
  • Endopeptidases
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex