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To study emissions of CO2 in the Baltimore, MD‐Washington, D.C. (Balt‐Wash) area, an aircraft campaign was conducted in February 2015, as part of the Fluxes of Atmospheric Greenhouse‐Gases in Maryland (FLAGG‐MD) project. During the campaign, elevated mole fractions of CO2 were observed downwind of the urban center and local power plants. Upwind flight data and Hybrid Single Particle Lagrangian Integrated Trajectory (HYSPLIT) model analyses help account for the impact of emissions outside the Balt‐Wash area. The accuracy, precision, and sensitivity of CO2 emissions estimates based on the mass balance approach were assessed for both power plants and cities. Our estimates of CO2 emissions from two local power plants agree well with their Continuous Emissions Monitoring Systems (CEMS) records. For the 16 power plant plumes captured by the aircraft, the mean percentage difference of CO2 emissions was −0.3%. For the Balt‐Wash area as a whole, the 1𝜎 CO2 emission rate uncertainty for any individual aircraft‐based mass balance approach experiment was ±38%. Treating the mass balance experiments, which were repeated seven times within 9 days, as individual quantifications of the Balt‐Wash CO2 emissions, the estimation uncertainty was ±16% (standard error of the mean at 95% CL). Our aircraft‐based estimate was compared to various bottom‐up fossil fuel CO2 (FFCO2) emission inventories. Based on the FLAGG‐MD aircraft observations, we estimate 1.9 ± 0.3 MtC of FFCO2 from the Balt‐Wash area during the month of February 2015. The mean estimate of FFCO2 from the four bottom‐up models was 2.2 ± 0.3 MtC. Key Points: 1.9 ± 0.3 MtC of fossil fuel CO2 was emitted in Baltimore‐Washington during February 2015 based on data collected during seven aircraft flightsFour bottom‐up inventories indicate 2.2 ± 0.3 MtC of fossil fuel CO2 was emitted, in good agreement with our top‐down estimateThe uncertainty from a single flight segment was ±38% (1𝜎); data from seven flights yielded a precision of 16% at the 95% confidence level [ABSTRACT FROM AUTHOR]

The vacancy doped p-type narrow band semiconductor of Hg0.73Cd0.27Te was characterized by ultra-high vacuum scanning tunneling microscopy (STM) and spectroscopy. The imaging displays surprisingly different topographies for positive and negative imaging biases, between which the observed surface pits with the negative bias are few tens nanometers shallower than their counterparts with the positive bias. The effect is subjected to two different local tunneling mechanisms which are not solely dictated by surface electronic properties. The observation contrasts with the conventional geometric view of the nanometer-scale corrugation of STM topography. [ABSTRACT FROM AUTHOR]

The Slit protein guides neuronal and leukocyte migration through the transmembrane receptor Roundabout (Robo). We report here that the intracellular domain of Robo interacts with a novel family of Rho GTPase activating proteins (GAPs). Two of the Slit-Robo GAPs (srGAPs) are expressed in regions responsive to Slit. Slit increased srGAP1-Robo1 interaction and inactivated Cdc42. A dominant negative srGAP1 blocked Slit inactivation of Cdc42 and Slit repulsion of migratory cells from the anterior subventricular zone (SVZa) of the forebrain. A constitutively active Cdc42 blocked the repulsive effect of Slit. These results have demonstrated important roles for GAPs and Cdc42 in neuronal migration. We propose a signal transduction pathway from the extracellular guidance cue to intracellular actin polymerization.

Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK2) are structurally related tyrosine kinases. They are implicated in regulating actin cytoskeleton organization, a process critical for cell migration, mitosis and tumor metastasis. In this paper, we demonstrate that, although both PYK2 and FAK were expressed and colocalized at focal adhesions in fibroblasts, microinjection of PYK2, but not FAK, in Swiss 3T3 fibroblastic cells led to reorganization of focal adhesions and cell rounding. PYK2-mediated actin cytoskeleton reorganization required the PYK2 N terminus, the focal adhesion targeting (FAT) domain, catalytic activity and autophosphorylation. Remarkably, FAK suppressed PYK2-mediated reorganization of focal adhesions and cell rounding. In addition, FAK inhibited PYK2 autophosphorylation and focal adhesion targeting, which might contribute to FAK-mediated suppression of PYK2's phenotypes. Further analyses demonstrated that the inhibition of PYK2 autophosphorylation required the FAK N terminus but not FAK tyrosine phosphorylation. The FAK FAT domain seemed to be critical for FAK-mediated suppression of PYK2 focal adhesion targeting. Taken together, these results demonstrate that FAK could inhibit PYK2 autophosphorylation, focal adhesion targeting and actin cytoskeleton reorganization, suggesting that the balance between FAK and PYK2 tyrosine kinases is important for regulating cellular morphology, cell migration and cell growth.

Proline-rich tyrosine kinase 2 (PYK2), a tyrosine kinase structurally related to focal adhesion kinase (FAK), is implicated in regulating cytoskeletal organization. However, mechanisms by which PYK2 participates in and regulates cytoskeletal organization remain largely unknown. Here we report identification of PSGAP, a novel protein that interacts with PYK2 and FAK and contains multiple domains including a pleckstrin homology domain, a rhoGTPase-activating protein domain, and a Src homology 3 domain. PYK2 interacts with PSGAP Src homology 3 domain via the carboxyl-terminal proline-rich sequence. PSGAP is able to increase GTPase activity of CDC42 and RhoA in vitro and in vivo. Remarkably, PYK2, but not FAK, can activate CDC42 via inhibition of PSGAP-mediated GTP hydrolysis of CDC42. Moreover, PSGAP is localized at cell periphery in fibroblasts in a pleckstrin homology domain-dependent manner. Over expression of PSGAP in fibroblasts results in reorganization of cytoskeletal structures and changes of cellular morphology, which requires rhoGTPase-activating activity. Taken together, our results suggest that PSGAP is a signaling protein essential for PYK2 regulation of cytoskeletal organization via Rho family GTPases.