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Biology subjects

Pick, J.

Publications and source records attributed to Pick, J..

2 recordsLinked to original sources

Examining the genetic and phenotypic correlation between survival and fecundity in a wild bird

There is intraspecific variation in reproduction and survival, which has been hypothesised to be the result of trade-offs in investment. However, we lack compelling evidence that trade- offs drive variation within species, perhaps because genetic trade-offs are masked by environmental variation. We used a long-term dataset of breeding records for a closed population of house sparrows (Passer domesticus) and its associated pedigree to separate the genetic and environmental covariance between fecundity and survival. We measured age-specific changes in reproductive outputs and estimated the heritability of both offspring production and survival in multivariate animal models. Our results show no evidence for survival costs to reproductive output. Nor did we find evidence that individuals fecundity and survival are correlated either the genetic or permanent environment level. Our findings show no evidence that variation in fecundity is driven by the offspring-production/survival trade-off. Instead, our results show that individuals are only somewhat consistent in their reproductive output, and suggest this is a possible mechanism why selection cannot act on individual quality.

evolutionary biology↗

The crystal structure of TRPM2 MHR1/2 domain reveals a conserved Zn2+-binding domain essential for ligand binding and activity

Transient receptor potential melastatin 2 (TRPM2) is a Ca2+-permeable, non-selective cation channel involved in diverse physiological processes such as immune response, apoptosis and body temperature sensing. TRPM2 is activated by ADP-ribose (ADPR) and 2'-deoxy-ADPR in a Ca2+-dependent manner. While two species-specific binding sites exist for ADPR, a binding site for 2'-deoxy-ADPR is not known yet. Here, we report the crystal structure of the MHR1/2 domain of TRPM2 from zebrafish (Danio rerio) and show binding of both ligands to this domain. We identified a so-far unrecognized Zn2+-binding domain that was not resolved in previous cryo-EM structures and that is conserved in most TRPM channels. In combination with patch clamp experiments, we comprehensively characterize the effect of the Zn2+-binding domain on TRPM2 activation. Our results provide insight into a conserved structural element essential for channel activity.

biochemistry↗