Cytosol as battleground: ubiquitin as a weapon for both host and pathogen.
Ubiquitin was first described as a tag allowing cells to degrade and recycle their own proteins. Recent research has shown ubiquitin to be central for immune system recognition of invading bacteria. This review describes a set of complex host-pathogen interactions that are dependent on ubiquitination. From the host perspective, ubiquitin-dependent activation of inflammation and degradation of bacterial effectors is protective. Several pathogens become ubiquitinated in the host cell cytosol, and recent research suggests that this could trigger a form of autophagy, increasingly recognized as an important mechanism for the control of infection by a variety of human pathogens. Meanwhile, bacteria have developed mechanisms to evade or exploit the fundamental processes activated by ubiquitination, producing both ubiquitin ligases and deubiquitinases that modulate host responses.
Medical Scientist Training Program, University of California San Francisco, San Francisco, CA 94143-0662, USA.
Cathleen A
CA
Collins
Eric J
EJ
Brown
D001343:Autophagy; D001419:Bacteria / Q000201:enzymology / Q000378:metabolism* / Q000472:pathogenicity; D001424:Bacterial Infections / Q000276:immunology* / Q000382:microbiology; D003600:Cytosol / Q000378:metabolism / Q000382:microbiology*; D054884:Host-Pathogen Interactions; D006801:Humans; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D057149:Ubiquitinated Proteins / Q000378:metabolism*; D054875:Ubiquitination; D014774:Virulence; D037521:Virulence Factors / Q000378:metabolism
D025801:Ubiquitin; D057149:Ubiquitinated Proteins; D037521:Virulence Factors; D044767:Ubiquitin-Protein Ligases