We have cloned a member of the STE20/SPS1 protein kinase family from a transformed rat pancreatic beta cell line. SPAK (STE20/SPS1-related, proline alanine-rich kinase) belongs to the SPS1 subfamily of STE20 kinases and is highly conserved between species. SPAK is expressed ubiquitously, although preferentially in brain and pancreas. Biochemical characterization of SPAK catalytic activity demonstrates that is a serine/threonine kinase that can phosphorylate itself and an exogenous substrate in vitro. SPAK is immunoprecipitated from transfected mammalian cells as a complex with another, as yet uncharacterized, serine/threonine kinase which is capable of phosphorylating catalytically-inactive SPAK and myelin basic protein in an in vitro kinase assay. SPAK speci®cally activates the p38 pathway in cotransfection assays. Like MST1 and MST2, SPAK contains a putative caspase cleavage site at the junction of the catalytic domain and the C-terminal region. Fulllength SPAK is expressed in the cytoplasm in transfected cells, while a mutant corresponding to caspase-cleaved SPAK is expressed predominantly in the nucleus. The similarity of SPAK to other SPS1 family members, its ability to activate the p38 pathway, in addition to its putative caspase cleavage site, provide evidence that SPAK may act as a novel mediator of stress-activated signals. Oncogene (2000) 19, 4290 ± 4297.

From 1973From to 1976From , 2430 blue cod (Parapercis colias) were tagged in the Marlborough Sounds. Tags from 84 fish (3.5%) were returned, after a mean 138 days at liberty. Of these, 71.6% had not moved significant distances. The remainder had travelled up to 41.7 km. Tag shedding rates, as indicated by multiple-tagging experiments, were high. Results suggest that blue cod of the Marlborough Sounds and the adjacent islands belong to the same stock, and that, while some move significant distances, the majority stay in 1 place for extended periods.

No abstract