Salvage logging and replanting reduce understory cover and richness compared to unsalvaged unplanted sites at Mount St. Helens, Washington

The 1980 eruption of Mount St. Helens killed trees in a broad 600-km2 swath north of the crater. Over most of the blast zone, dead trees were salvage logged and Abies procera was planted, except in areas within the Mount St. Helens National Volcanic Monument. We compared salvage-replanted sites and unsalvaged sites in 1 area of the blast zone where the sites were adjacent by using twenty-five 200-m 2 plots for each treatment. Salvaged-replanted plots had significantly lower herb and shrub cover, richness, diversity, litter depth, downed woody debris, nitrate, and phosphate. Salvaged-replanted sites also had significantly more stumps, bare area, and moss cover than unsalvaged plots. Soil organic matter and nonnative species cover did not differ. Nonnative species were not important components of any plots. Nitrate, total nitrogen, organic matter, and litter were correlated with the major patterns of species distribution in a canonical correspondence analysis of the salvaged-replanted plots. In the unsalvaged plots, slope, downed woody debris, and elevation were correlated with the major patterns of species distribution.     

Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease

Mice that are homozygous with respect to a mutation (ax(J)) in the ataxia (ax) gene develop severe tremors by 2-3 weeks of age followed by hindlimb paralysis and death by 6-10 weeks of age. Here we show that ax encodes ubiquitin-specific protease 14 (Usp14). Ubiquitin proteases are a large family of cysteine proteases that specifically cleave ubiquitin conjugates. Although Usp14 can cleave a ubiquitin-tagged protein in vitro, it is unable to process polyubiquitin, which is believed to be associated with the protein aggregates seen in Parkinson disease, spinocerebellar ataxia type 1 (SCA1; ref. 4) and gracile axonal dystrophy (GAD). The physiological substrate of Usp14 may therefore contain a mono-ubiquitin side chain, the removal of which would regulate processes such as protein localization and protein activity. Expression of Usp14 is significantly altered in ax(J)/ax(J) mice as a result of the insertion of an intracisternal-A particle (IAP) into intron 5 of Usp14. In contrast to other neurodegenerative disorders such as Parkinson disease and SCA1 in humans and GAD in mice, neither ubiquitin-positive protein aggregates nor neuronal cell loss is detectable in the central nervous system (CNS) of ax(J) mice. Instead, ax(J) mice have defects in synaptic transmission in both the central and peripheral nervous systems. These results suggest that ubiquitin proteases are important in regulating synaptic activity in mammals.