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MOTIVATION: We undertook large citizen science surveys of bird distributions (atlases) in Britain and Ireland, aimed at quantifying breeding bird distributions on a 20‐year cycle and wintering bird distributions on a c. 30‐year cycle. We use these to generate spatially referenced information on apparent changes in bird distributions over c. 40 years. MAIN TYPE OF VARIABLE CONTAINED: Detection of breeding and wintering bird species in grid squares during five periods, and changes in detection between periods. The combined distribution dataset contains 1,410,938 records detailing detections of 465 bird species in 3,880 grid cells in different periods. The combined distribution change dataset contains 1,297,791 records describing stability, apparent colonization or apparent extinction of individual species in grid squares between pairs of atlases spanning up to c. 40 years. SPATIAL LOCATION AND GRAIN: Grid squares (10 km × 10 km) containing land throughout Britain, Ireland, the Isle of Man and the Channel Islands. The majority of data are at 10‐km resolution, but data for rare species are summarized at 20‐ or 50‐km resolution to protect sensitive locations. TIME PERIOD: The data represent summarized detection information derived from fieldwork during five periods: the breeding seasons 1968–1972, 1988–1991 and 2008–2011, and the winters 1981/1982–1983/1984 and 2007/2008–2010/2011. MAJOR TAXA STUDIED AND LEVEL OF MEASUREMENT: Birds; their distribution derived from citizen science surveys. SOFTWARE FORMAT: Data are supplied as comma‐separated text files.

PTEN, a tumor suppressor among the most commonly mutated proteins in human cancer, is recognized to be both a protein phosphatase and a phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P 3 ) 3-phosphatase. Previous work [Maehama and Dixon, J. Biol. Chem. 273 (1998) 13375–13378] has led to a consensus that inositol phosphates are not physiologically relevant substrates for PTEN. In contrast, we demonstrate that PTEN is an active inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P 5 ) 3-phosphatase when expressed and purified from bacteria or HEK cells. Kinetic data indicate Ins(1,3,4,5,6)P 5 ( K m =7.1 μM) and PtdIns(3,4,5)P 3 ( K m =26 μM) compete for PTEN in vivo. Transient transfection of HEK cells with PTEN decreased Ins(1,3,4,5,6)P 5 levels. We discuss the physiological significance of these studies in relation to recent work showing that dephosphorylation of Ins(1,3,4,5,6)P 5 to inositol 1,4,5,6-tetrakisphosphate is a cell signaling event.

The ARGRIII gene of Saccharomyces cerevisiae encodes a transcriptional regulator that also has inositol polyphosphate multikinase (ipmk) activity [Saiardi et al. (1999) Curr. Biol. 9, 1323-1326]. To investigate how inositol phosphates regulate gene expression, we disrupted the ARGRIII gene. This mutation impaired nuclear mRNA export, slowed cell growth, increased cellular [InsP(3)] 170-fold and decreased [InsP(6)] 100-fold, indicating reduced phosphorylation of InsP(3) to InsP(6). Levels of diphosphoinositol polyphosphates were decreased much less dramatically than was InsP(6). Low levels of InsP(6), and considerable quantities of Ins(1,3,4,5)P(4), were synthesized by an ipmk-independent route. Transcriptional control by ipmk reflects that it is a pivotal regulator of nuclear mRNA export via inositol phosphate metabolism.

We have derived the full-length sequences of the human and rat forms of the multiple inositol polyphosphate phosphatase (MIPP); their structural and functional comparison with a chick histidine acid phosphatase (HiPER1) has revealed new information: (1) MIPP is approximately 50% identical to HiPER1, but the ER-targeting domains are divergent; (2) MIPP appears to share the catalytic requirement of histidine acid phosphatases, namely, a C-terminal His residue remote from the RHGxRxP catalytic motif; (3) rat MIPP mRNA is up-regulated during chondrocyte hypertrophy. The latter observation provides a context for proposing that MIPP may aid bone mineralization and salvage the inositol moiety prior to apoptosis.