(Re)Storying Obama: An Examination of Recently Published Informational Texts

American publishers have published numerous children’s books about Barack Obama over the past several years; most take the form of informational biographies. This article reports on a research project aimed at how these books incorporate sociohistorical narratives, particularly those related to the civil rights movement. Though the features of the books might cause the reader to presume political neutrality, the books link readers to distinct Discourses (Gee, 1996), suggesting particular ideologies. In this article, we identified the following differences: (1) specific happenings from Obama’s life were included in some texts while omitted in others; (2) when the events were included, how they were framed differed; and (3) the narrative constructions of the events varied. We use the differences amongst these texts to argue for the importance of critical literacy in elementary classrooms

Phosphorylation At Ser244 By Ck1 Determines Nuclear Localization And Substrate Targeting Of Pkd2

Protein kinase D2 (PKD2), a member of the PKD family of serine/threonine kinases, is localized in various subcellular compartments including the nucleus where the kinase accumulates upon activation of G-protein-coupled receptors. We define three critical post-translational modifications required for nuclear accumulation of PKD2 in response to activation of the CCK2 receptor (CCK2R): phosphorylation at Ser706 and Ser710 within the activation loop by PKC eta leading to catalytic activity and phosphorylation at Ser244 within the zinc-finger domain, which is crucial for blocking nuclear export of active PKD2 by preventing its interaction with the Crm-1 export machinery. We identify CK1delta and epsilon as upstream activated kinases by CCK2R that phosphorylate PKD2 at Ser244. Moreover, nuclear accumulation of active PKD2 is a prerequisite for efficient phosphorylation of its nuclear substrate, HDAC7. Only nuclear, active PKD2 mediates CCK2R-induced HDAC7 phosphorylation and Nur77 expression. Thus, we define a novel, compartment-specific signal transduction pathway downstream of CCK2R that phosphorylates PKD2 at three specific sites, results in nuclear accumulation of the active kinase and culminates in efficient phosphorylation of nuclear PKD2 substrates in human gastric cancer cells