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Oz, I.

Publications and source records attributed to Oz, I..

2 recordsLinked to original sources

Evidence for efficient non-evaporative leaf-to-air heat dissipation in a pine forest under drought conditions

O_LIDrier climates predicted for many regions can result in reduced evaporative cooling leading to leaf heat stress and enhanced mortality. To what extent non-evaporative cooling can contribute to plant resilience to the increasingly stressful conditions is poorly known at present. C_LIO_LIUsing a novel, high accuracy infrared system for continuous measurements of leaf temperature in mature trees under field conditions, we assessed leaf-to-air temperature differences {Delta}Tleaf-air of pine needles during drought. C_LIO_LIOn mid-summer days, {Delta}Tleaf-air remained <1.5 {degrees}C, both in trees exposed to summer drought, and in those provided with a supplement irrigation having a 10x higher transpiration rate. The non-evaporative cooling in the drought-exposed trees must be facilitated by low resistance to heat transfer generating large H. {Delta}Tleaf-air was weakly related to variations in the radiation load and mean wind speed in the lower part of the canopy, but highly dependent on canopy structure and within-canopy turbulence that enhanced the sensible heat flux H. C_LIO_LINon-evaporative cooling is demonstrated as an effective cooling mechanism in needle-leaf trees, which can be a critical factor in forest resistance to drying climates. The generation of a large H at the leaf scale provides a basis for the development of the previously identified canopy-scale convector effect. C_LI

physiology

Itk promotes the integration of TCR and CD28 costimulation, through its direct substrates, SLP-76 and Gads

The costimulatory receptor, CD28, synergizes with the T cell antigen receptor (TCR) to promote IL-2 production, cell survival and proliferation. Despite their profound synergy, the obligatory interdependence of the signaling pathways initiated by these two receptors is not well understood. Upon TCR stimulation, Gads, a Grb2-family adaptor, bridges the interaction of two additional adaptors, LAT and SLP-76, to form a TCR-induced effector signaling complex. SLP-76 binds the Tec-family tyrosine kinase, Itk, which phosphorylates SLP-76 at Y173 and PLC-{gamma}1 at Y783. Here we identified Gads Y45 as an additional TCR-inducible, Itk-mediated phosphorylation site. Y45 is found within the N-terminal SH3 domain of Gads, an evolutionarily conserved domain with no known binding partners or signaling function. Gads Y45 phosphorylation depended on the interaction of Gads with SLP-76 and on the preferentially-paired binding of Gads to phospho-LAT. Three Itk-related features, Gads Y45, SLP-76 Y173, and a proline-rich Itk SH3-binding motif on SLP-76, were selectively required for activation of the CD28 RE/AP transcriptional element from the IL-2 promoter, but were not required to activate NFAT. This study illuminates a new regulatory module, in which Itk-targeted phosphorylation sites on two adaptor proteins, SLP-76 and Gads, control the transcriptional response to TCR/CD28 costimulation, thus enforcing the obligatory interdependence of the TCR and CD28 signaling pathways.

immunology