Vacuolar proteases livening up programmed cell death.
The molecular identity of the key executioners involved in controlling plant programmed cell death (PCD) has been elusive. In a recent paper published in Science, Hatsugai and coworkers reported that a well-characterized protease called VPE from the plant cell vacuole can cleave caspase-specific substrates and is required for cell death activation by tobacco mosaic virus. This work provides clear evidence for the importance of the vacuole in plant PCD and a novel regulatory function for this organelle as well as for VPE proteases.
Lam
Eric
E
Biotech Center, Rutgers University, 59 Dudley Road, Foran Hall, New Brunswick, NJ 08901, USA. Lam@aesop.rutgers.edu
D017360:Arabidopsis / Q000378:metabolism; D016923:Cell Death; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D008957:Models, Genetic; D010447:Peptide Hydrolases / Q000502:physiology*; D010935:Plant Diseases; D010940:Plant Proteins / Q000378:metabolism / Q000502:physiology*; D015398:Signal Transduction; D014027:Tobacco Mosaic Virus / Q000378:metabolism; D014617:Vacuoles / Q000201:enzymology*; D000099240:Asparaginyl Endopeptidase
D003546:Cysteine Endopeptidases; D010447:Peptide Hydrolases; D010940:Plant Proteins; D000099240:Asparaginyl Endopeptidase