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1.
Hist Philos Life Sci ; 42(1): 2, 2019 Dec 31.
Artigo em Inglês | MEDLINE | ID: mdl-31893315

RESUMO

Although the buying, selling, and trading of fossils has been a principle part of paleontological practice over the centuries, the commercial collection of fossils today has re-emerged into a pervasive and lucrative industry. In the United States, the number of commercial companies driving the legal, and sometimes illegal, selling of fossils is estimated to have doubled since the 1980s, and worries from academic paleontologists over this issue has increased accordingly. Indeed, some view the commercialization of fossils as one of the greatest threats to paleontology today. In this article, I address the story of "Sue"-the largest, most complete, and most expensive Tyrannosaurus rex ever excavated-whose discovery incited a series of high-profile legal battles throughout the 1990s over the question of "Who owns Sue?" Over the course of a decade, various stakeholders from academic paleontologists and fossil dealers to Native Americans, private citizens, and government officials all laid claim to Sue. In exploring this case, I argue that assumptions of authority are responsible for initiating and sustaining debates over fossil access. Here, assumptions of authority are understood as assumptions of ownership, or expertise, or in some cases both. Viewing the story from this perspective illuminates the significance of fossils as boundary objects. It also highlights the process of boundary-work by which individuals and groups constructed or deconstructed borders around Sue (specifically) and fossil access (more generally) to establish their own authority. I draw on science studies scholarship as well as literature in the professionalization, commercialization, and valuation of science to examine how assumptions of authority facilitated one of the most divisive episodes in recent paleontological history and the broader debate on the commercial collection of vertebrate fossil material in the United Sates.


Assuntos
Fósseis/história , Propriedade , Paleontologia/história , Animais , Dinossauros , História do Século XX , História do Século XXI , Manejo de Espécimes/história
2.
Mol Cell Biol ; 27(19): 6913-32, 2007 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-17646391

RESUMO

The steroid receptor coactivator 3 gene (SRC-3) (AIB1/ACTR/pCIP/RAC3/TRAM1) is a p160 family transcription coactivator and a known oncogene. Despite its importance, the functional regulation of SRC-3 remains poorly understood within a cellular context. Using a novel combination of live-cell, high-throughput, and fluorescent microscopy, we report SRC-3 to be a nucleocytoplasmic shuttling protein whose intracellular mobility, solubility, and cellular localization are regulated by phosphorylation and estrogen receptor alpha (ERalpha) interactions. We show that both chemical inhibition and small interfering RNA reduction of the mitogen-activated protein kinase/extracellular signal-regulated kinase 1/2 (MEK1/2) pathway induce a cytoplasmic shift in SRC-3 localization, whereas stimulation by epidermal growth factor signaling enhances its nuclear localization by inducing phosphorylation at T24, S857, and S860, known participants in the phosphocode that regulates SRC-3 activity. Accordingly, the cytoplasmic localization of a nonphosphorylatable SRC-3 mutant further supported these results. In the presence of ERalpha, U0126 also dramatically reduces (i) ligand-dependent colocalization of SRC-3 and ERalpha, (ii) the formation of ER-SRC-3 complexes in cell lysates, and (iii) SRC-3 targeting to a visible, ERalpha-occupied and -regulated prolactin promoter array. Taken together, these results indicate that phosphorylation coordinates SRC-3 coactivator function by linking the probabilistic formation of transient nuclear receptor-coactivator complexes with its molecular dynamics and cellular compartmentalization. Technically and conceptually, these findings have a new and broad impact upon evaluating mechanisms of action of gene regulators at a cellular system level.


Assuntos
Histona Acetiltransferases/metabolismo , Receptores de Estrogênio/metabolismo , Frações Subcelulares/metabolismo , Transativadores/metabolismo , Transporte Ativo do Núcleo Celular/fisiologia , Animais , Linhagem Celular , Núcleo Celular/metabolismo , Citoplasma/metabolismo , Retículo Endoplasmático/metabolismo , Fator de Crescimento Epidérmico/metabolismo , MAP Quinases Reguladas por Sinal Extracelular/metabolismo , Histona Acetiltransferases/genética , Histona Acetiltransferases/ultraestrutura , Humanos , Imuno-Histoquímica , Proteínas Nucleares/genética , Proteínas Nucleares/metabolismo , Proteínas Nucleares/ultraestrutura , Coativador 3 de Receptor Nuclear , Fosforilação , Regiões Promotoras Genéticas , Interferência de RNA , Receptores de Estrogênio/genética , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Transdução de Sinais/fisiologia , Frações Subcelulares/ultraestrutura , Transativadores/genética , Transativadores/ultraestrutura
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