Photography-based taxonomy is inadequate, unnecessary, and potentially harmful for biological sciences

The question whether taxonomic descriptions naming new animal species without type specimen(s) deposited in collections should be accepted for publication by scientific journals and allowed by the Code has already been discussed in Zootaxa (Dubois & Nemésio 2007; Donegan 2008, 2009; Nemésio 2009a–b; Dubois 2009; Gentile & Snell 2009; Minelli 2009; Cianferoni & Bartolozzi 2016; Amorim et al. 2016). This question was again raised in a letter supported by 35 signatories published in the journal Nature (Pape et al. 2016) on 15 September 2016. On 25 September 2016, the following rebuttal (strictly limited to 300 words as per the editorial rules of Nature) was submitted to Nature, which on 18 October 2016 refused to publish it. As we think this problem is a very important one for zoological taxonomy, this text is published here exactly as submitted to Nature, followed by the list of the 493 taxonomists and collection-based researchers who signed it in the short time span from 20 September to 6 October 2016

Le domaine N-terminal des recepteurs nucléaires des rétinoïdes (Phosphorylation et mise en évidence de nouveaux corégulateurs)

Les rétinoïdes (dérivés de la vitamine A) agissent via deux familles de récepteurs nucléaires: les RAR (a, b, g) et les RXR (a, b, g). Ces récepteurs sont des activateurs de la transcription inductibles par leur ligand dont l'activité est régulée par le recrutement dynamique de complexes protéiques au niveau de leur domaine AF-2. Il a été démontré récemment dans l'équipe que les RAR sont aussi des cibles pour des processus de phosphorylation. J'ai montré que l'efficacité de la phosphorylation du domaine AF-1 par la kinase cdk7 dépend de la fixation, au niveau du domaine AF-2, de la cycline H au sein du complexe CAK. De manière symétrique, j'ai montré que la phosphorylation du domaine AF-2 par la PKA, au niveau d'un résidu proche du site de l'interaction de la cycline H, augmente la phosphorylation du domaine AF-1 par cdk7, ainsi que la transcription de gènes cibles. Ces résultats démontrent une coopération entre les domaines AF-1 et AF-2 par des processus de phosphorylation. Dans le cas de RARg, une sérine supplémentaire du domaine AF-1 est phosphorylée par la p38MAPK en réponse aux rétinoïdes. La phosphorylation par cdk7 ainsi que celle par la p38MAPK sont nécessaires à l'activité transcriptionnelle maximale de RARg. Pour comprendre le rôle de ces processus de phosphorylation dans la transcription, je me suis attaché à identifier des partenaires du domaine AF-1 de RARg en fonction de son état de phosphorylation. J'ai ainsi identifié la vinexine b, une protéine adaptatrice appartenant à la famille des Vinexine, CAP/Ponsin, ArgBP2, initialement impliquée dans l'organisation du cytosquelette, l'adhérence des cellules au niveau des adhérences focales ainsi que dans la transduction des signaux. Mes travaux montrent que cette protéine peut aussi être présente dans le noyau et y contrôler de façon négative la transcription des gènes cibles de RARg.STRASBOURG-Sc. et Techniques (674822102) / SudocSudocFranceF

Recent avian extinctions on Réunion (Mascarene Islands) from paleontological and historical sources

International audienceThe Mascarene Islands were uninhabited when the first Europeans settled there, during the 16th century. The strange avifauna of these islands was described by the early travellers, but many species disappeared very rapidly. Fossil remains were discovered very early on Rodrigues, and later on Mauritius, but it was only in 1974 that the first remains of fossil birds were discovered on Réunion, in a large cave,‘Grotte des Premiers Français'. Subsequently, other remains were discovered in small basaltic caves and in a marsh. These fossil birds were studied by Cowles (1987, 1994), Mourer-Chauviré & Moutou (1987), Mourer-Chauviré et al. (1994, 1995a,b), following which a comprehensive paper concerning the different species and fossiliferous localities was issued (Mourer-Chauviré et al. 1999). The original avifauna of Réunion is also known from the accounts of early visitors, whose reports were collated by Lougnon (1970). The parts concerning birds are also presented by Barré & Barau (1982) and Barré et al. (1996). Particular parts of these accounts were discussed by Cheke (1987), and a previously unknown report, by Melet, who called at Réunion in 1671, was discovered by Anne Sauvaget and published in 1999 (Sauvaget 1999)

Protein kinases and the proteasome join in the combinatorial control of transcription by nuclear retinoic acid receptors.

Nuclear retinoic acid receptors (RARs) are transcriptional transregulators that control the expression of specific subsets of genes in a ligand-dependent manner. The basic mechanism for switching on gene transcription by agonist-liganded RARs involves their binding at specific response elements located in target genes. It also involves interactions with coregulatory protein complexes, the assembly of which is directed by the C-terminal ligand-binding domain of RARs. In addition to this scenario, several recent studies highlighted a fundamental role for the N-terminal domain in the transcriptional activity of RARs, following phosphorylation by the CDK7 kinase of the general transcription factor TFIIH and by p38MAPK. It has also emerged that the ubiquitin-proteasome system has a key role in RAR-mediated transcription. Here, we review new insights into how N-terminal domain and the proteasome pathway can influence the dynamics of RAR transcriptional activity

Vinexin beta interacts with the non-phosphorylated AF-1 domain of retinoid receptor gamma (RARgamma) and represses RARgamma-mediated transcription.

International audienceNuclear retinoic acid receptors (RARs) are ligand-dependent transcription factors that regulate the expression of retinoic acid target genes. Although the importance of RAR phosphorylation in their N-terminal domain is clearly established, the underlying mechanism for the phosphorylation-dependent transcriptional activity of the receptors had not been elucidated yet. Here, using a yeast two-hybrid system, we report the isolation of vinexin beta as a new cofactor that interacts with the N-terminal A/B domain of the RARgamma isotype. Vinexin beta is a multiple SH3 motif-containing protein associated with the cytoskeleton and also present in the nucleus. We demonstrate that vinexin beta colocalizes with RARgamma in the nucleus and interacts with the non-phosphorylated form of the AF-1 domain of RARgamma. We also show that this interaction is prevented upon phosphorylation of the AF-1 domain. Using F9 cells stably overexpressing vinexin beta or vinexin knockdown by RNA interference, we demonstrate that vinexin beta is an inhibitor of RARgamma-mediated transcription. We propose a model in which phosphorylation of the AF-1 domain controls RARgamma-mediated transcription through triggering the dissociation of vinexin beta

Cenozoic landforms and post-orogenic evolution of the Balkanide orogen: evidence for alternatives to the tectonic denudation narrative in southern Bulgaria

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Different meteorological parameters influence metapneumovirus and respiratory syncytial virus activity

International audienceBackgroundBoth human metapneumovirus (hMPV) and respiratory syncytial virus (RSV) cause epidemics during the cold season in temperate climates.ObjectivesThe purpose of this study was to find out whether climatic factors are associated with RSV and hMPV epidemics.Study designOur study was based on data from 4300 patients admitted to the Dijon University Hospital for acute respiratory infection (ARI) over three winter seasons chosen for their dissimilar meteorological and virological patterns. Cases of hMPV and RSV were correlated with meteorological parameters recorded in the Dijon area. The relationship between virus data and local meteorological conditions was analyzed by univariate and multivariate negative binomial regression analysis.ResultsRSV detection was inversely associated with temperature and positively with relative humidity and air pressure, whereas hMPV was inversely associated with temperature and positively with wind speed.ConclusionsThe association among meteorological variables and weekly ARIs cases due to RSV and hMPV demonstrated the relevance of climate factors as contributors to both hMPV and RSV activities. Meteorological drivers of RSV and hMPV epidemics are different. Low temperatures influence both hMPV and RSV activity. Relative humidity is an important predictor of RSV activity, but it does not influence hMPV activity

Cyclin H binding to the RARalpha activation function (AF)-2 domain directs phosphorylation of the AF-1 domain by cyclin-dependent kinase 7.

International audienceThe transcriptional activity of nuclear retinoic acid receptors (RARs), which act as RAR/retinoid X receptor (RXR) heterodimers, depends on two activation functions, AF-1 and AF-2, which are targets for phosphorylations and synergize for the activation of retinoic acid target genes. The N-terminal AF-1 domain of RARalpha is phosphorylated at S77 by the cyclin-dependent kinase (cdk)-activating kinase (CAK) subcomplex (cdk7/cyclin H/MAT1) of the general transcription factor TFIIH. Here, we show that phosphorylation of S77 governing the transcriptional activity of RARalpha depends on cyclin H binding at a RARalpha region that encompasses loop 8-9 and the N-terminal tip of helix 9 of the AF-2 domain. We propose a model in which the structural constraints of this region control the architecture of the RAR/RXR/TFIIH complex and therefore the efficiency of RARalpha phosphorylation by cdk7. To our knowledge, this study provides the first example of a cooperation between the AF-2 and AF-1 domains of RARs through a kinase complex

Phosphorylation by PKA potentiates retinoic acid receptor α activity by means of increasing interaction with and phosphorylation by cyclin H/cdk7

Nuclear retinoic acid receptors (RARs) work as ligand-dependent heterodimeric RAR/retinoid X receptor transcription activators, which are targets for phosphorylations. The N-terminal activation function (AF)-1 domain of RARα is phosphorylated by the cyclin-dependent kinase (cdk) 7/cyclin H complex of the general transcription factor TFIIH and the C-terminal AF-2 domain by the cAMP-dependent protein kinase A (PKA). Here, we report the identification of a molecular pathway by which phosphorylation by PKA propagates cAMP signaling from the AF-2 domain to the AF-1 domain. The first step is the phosphorylation of S369, located in loop 9–10 of the AF-2 domain. This signal is transferred to the cyclin H binding domain (at the N terminus of helix 9 and loop 8–9), resulting in enhanced cyclin H interaction and, thereby, greater amounts of RARα phosphorylated at S77 located in the AF-1 domain by the cdk7/cyclin H complex. This molecular mechanism relies on the integrity of the ligand-binding domain and the cyclin H binding surface. Finally, it results in higher DNA-binding efficiency, providing an explanation for how cAMP synergizes with retinoic acid for transcription