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1.  Phenotypic and Genetic Divergence among Poison Frog Populations in a Mimetic Radiation 
PLoS ONE  2013;8(2):e55443.
The evolution of Müllerian mimicry is, paradoxically, associated with high levels of diversity in color and pattern. In a mimetic radiation, different populations of a species evolve to resemble different models, which can lead to speciation. Yet there are circumstances under which initial selection for divergence under mimicry may be reversed. Here we provide evidence for the evolution of extensive phenotypic divergence in a mimetic radiation in Ranitomeya imitator, the mimic poison frog, in Peru. Analyses of color hue (spectral reflectance) and pattern reveal substantial divergence between morphs. However, we also report that there is a “transition-zone” with mixed phenotypes. Analyses of genetic structure using microsatellite variation reveals some differentiation between populations, but this does not strictly correspond to color pattern divergence. Analyses of gene flow between populations suggest that, while historical levels of gene flow were low, recent levels are high in some cases, including substantial gene flow between some color pattern morphs. We discuss possible explanations for these observations.
doi:10.1371/journal.pone.0055443
PMCID: PMC3566184  PMID: 23405150
2.  Advergence in Müllerian mimicry: the case of the poison dart frogs of Northern Peru revisited 
Biology Letters  2011;7(5):796-800.
Whether the evolution of similar aposematic signals in different unpalatable species (i.e. Müllerian mimicry) is because of phenotypic convergence or advergence continues to puzzle scientists. The poison dart frog Ranitomeya imitator provides a rare example in support of the hypothesis of advergence: this species was believed to mimic numerous distinct model species because of high phenotypic variability and low genetic divergence among populations. In this study, we test the evidence in support of advergence using a population genetic framework in two localities where R. imitator is sympatric with different model species, Ranitomeya ventrimaculata and Ranitomeya variabilis. Genetic analyses revealed incomplete sorting of mitochondrial haplotypes between the two model species. These two species are also less genetically differentiated than R. imitator populations on the basis of both mitochondrial and nuclear DNA comparisons. The genetic similarity between the model species suggests that they have either diverged more recently than R. imitator populations or that they are still connected by gene flow and were misidentified as different species. An analysis of phenotypic variability indicates that the model species are as variable as R. imitator. These results do not support the hypothesis of advergence by R. imitator. Although we cannot rule out phenotypic advergence in the evolution of Müllerian mimicry, this study reopens the discussion regarding the direction of the evolution of mimicry in the R. imitator system.
doi:10.1098/rsbl.2011.0039
PMCID: PMC3169040  PMID: 21411452
phenotypic advergence; Ranitomeya; mimicry
3.  A Membrane Fusion Protein αSNAP Is a Novel Regulator of Epithelial Apical Junctions 
PLoS ONE  2012;7(4):e34320.
Tight junctions (TJs) and adherens junctions (AJs) are key determinants of the structure and permeability of epithelial barriers. Although exocytic delivery to the cell surface is crucial for junctional assembly, little is known about the mechanisms controlling TJ and AJ exocytosis. This study was aimed at investigating whether a key mediator of exocytosis, soluble N-ethylmaleimide sensitive factor (NSF) attachment protein alpha (αSNAP), regulates epithelial junctions. αSNAP was enriched at apical junctions in SK-CO15 and T84 colonic epithelial cells and in normal human intestinal mucosa. siRNA-mediated knockdown of αSNAP inhibited AJ/TJ assembly and establishment of the paracellular barrier in SK-CO15 cells, which was accompanied by a significant down-regulation of p120-catenin and E-cadherin expression. A selective depletion of p120 catenin effectively disrupted AJ and TJ structure and compromised the epithelial barrier. However, overexpression of p120 catenin did not rescue the defects of junctional structure and permeability caused by αSNAP knockdown thereby suggesting the involvement of additional mechanisms. Such mechanisms did not depend on NSF functions or induction of cell death, but were associated with disruption of the Golgi complex and down-regulation of a Golgi-associated guanidine nucleotide exchange factor, GBF1. These findings suggest novel roles for αSNAP in promoting the formation of epithelial AJs and TJs by controlling Golgi-dependent expression and trafficking of junctional proteins.
doi:10.1371/journal.pone.0034320
PMCID: PMC3317505  PMID: 22485163
4.  Tactical reproductive parasitism via larval cannibalism in Peruvian poison frogs 
Biology Letters  2008;5(2):148-151.
We report an unusual example of reproductive parasitism in amphibians. Dendrobates variabilis, an Amazonian poison frog, oviposits at the surface of the water in small pools in plants and deposits tadpoles within the pools. Tadpoles are highly cannibalistic and consume young tadpoles if they are accessible. Deposition of embryos and tadpoles in the same pool is common. Genetic analyses indicate that tadpoles are frequently unrelated to embryos in the same pool. A pool choice experiment in the field demonstrated that males carrying tadpoles prefer to place them in pools with embryos, facilitating reproductive parasitism via cannibalism.
doi:10.1098/rsbl.2008.0591
PMCID: PMC2665805  PMID: 19042178
reproductive parasitism; egg cannibalism; Dendrobates; Ranitomeya; deposition strategies; anuran
5.  Hydrolytic Enzyme Production by Rhizobium† 
Cellulase and hemicellulase activity was detected in temperate (infective and noninfective) and tropical strains (infective) of Rhizobium. Hydrolytic enzymes were initially detected by a cup-plate assay. The presence of cellulase and hemicellulase was confirmed by viscometric assay. Implications of the presence of these enzymes in Rhizobium are discussed.
PMCID: PMC291267  PMID: 16345483

Results 1-5 (5)