Nuclear dependence coefficient α(A,qT)\alpha(A,q_T) for the Drell-Yan and J/ψ\psi production

Define the nuclear dependence coefficient $\alpha(A,q_T)$ in terms of ratio of transverse momentum spectrum in hadron-nucleus and in hadron-nucleon collisions: $\frac{d\sigma^{hA}}{dq_T^2}/ \frac{d\sigma^{hN}}{dq_T^2}\equiv A^{\alpha(A,q_T)}$. We argue that in small $q_T$ region, the $\alpha(A,q_T)$ for the Drell-Yan and J/$\psi$ production is given by a universal function:\ $a+b q_T^2$, where parameters a and b are completely determined by either calculable quantities or independently measurable physical observables. We demonstrate that this universal function $\alpha(A,q_T)$ is insensitive to the A for normal nuclear targets. For a color deconfined nuclear medium, the $\alpha(A,q_T)$ becomes strongly dependent on the A. We also show that our $\alpha(A,q_T)$ for the Drell-Yan process is naturally linked to perturbatively calculated $\alpha(A,q_T)$ at large $q_T$ without any free parameters, and the $\alpha(A,q_T)$ is consistent with E772 data for all $q_T$.Comment: latex, 28 pages, 10 figures, updated two figures, and add more discussion

A simple event weighting technique for optimizing the measurement of the forward-backward asymmetry of Drell-Yan dilepton pairs at hadron colliders

We describe a simple technique for optimizing the extraction of the forward-backward asymmetry ($A_{fb}$) of Drell-Yan lepton pairs ($e^+e^-$,$\mu^+\mu^-$) produced in $\bar{p}p$ and $pp$ collisions at hadron colliders. The method employs simple event weights which are functions of the rapidity and $cos\theta$ decay angle of the lepton pair. It yields the best estimate of the acceptance corrected parton level ($\bar{q}q$) forward backward asymmetry as a function of final state dilepton mass ($M_{\ell\ell}$). Typically, when compared to the simple count method, the technique reduces the statistical errors by 20% for $\bar{p}p$, and 40% for $pp$ collisions, respectively. The technique can be used to search for new high mass and large width Z' bosons which may be best detected through the observation of deviations from the Standard Model expectation for the forward-backward asymmetry. In addition, we derive expressions for the QCD angular coefficients for Drell-Yan events.Comment: 13 pages, 1 figure, 4 tables. Accepted for publication in EPJ

Structure of the Golgi and Distribution of Reporter Molecules at 20°C Reveals the Complexity of the Exit Compartments

Incubating cells at 20°C blocks transport out of the Golgi complex and amplifies the exit compartments. We have used the 20°C block, followed by EM tomography and serial section reconstruction, to study the structure of Golgi exit sites in NRK cells. The dominant feature of Golgi structure in temperature-blocked cells is the presence of large bulging domains on the three trans-most cisternae. These domains extend laterally from the stack and are continuous with “cisternal” domains that maintain normal thickness and alignment with the other stacked Golgi cisternae. The bulging domains do not resemble the perpendicularly extending tubules associated with the trans-cisternae of control cells. Such tubules are completely absent in temperature-blocked cells. The three cisternae with bulging domains can be identified as trans by their association with specialized ER and the presence of clathrin-coated buds on the trans-most cisterna only. Immunogold labeling and immunoblots show a significant degradation of a medial- and a trans-Golgi marker with no evidence for their redistribution within the Golgi or to other organelles. These data suggest that exit from the Golgi occurs directly from three trans-cisternae and that specialized ER plays a significant role in trans-Golgi function

Localization of Large ADP-Ribosylation Factor-Guanine Nucleotide Exchange Factors to Different Golgi Compartments: Evidence for Distinct Functions in Protein Traffic

Activation of several ADP-ribosylation factors (ARFs) by guanine nucleotide exchange factors (GEFs) regulates recruitment of coat proteins (COPs) on the Golgi complex and is generally assumed to be the target of brefeldin A (BFA). The large ARF-GEFs Golgi-specific BFA resistance factor 1 (GBF1) and BFA-inhibited GEFs (BIGs) localize to this organelle but catalyze exchange preferentially on class II and class I ARFs, respectively. We now demonstrate using quantitative confocal microscopy that these GEFs show a very limited overlap with each other (15 and 23%). In contrast, GBF1 colocalizes with the cis-marker p115 (86%), whereas BIGs overlap extensively with TGN38 (83%). Consistent with these distributions, GBF1, but not BIG1, partially relocalized to peripheral sites after incubation at 15°C. The new GBF1 structures represent peripheral vesicular tubular clusters (VTCs) because 88% of structures analyzed stained for both GBF1 and p115. Furthermore, as expected of VTCs, they rapidly reclustered to the Golgi complex in a microtubule-dependent manner upon warm-up. These observations suggest that GBF1 and BIGs activate distinct subclasses of ARFs in specific locations to regulate different types of reactions. In agreement with this possibility, COPI overlapped to a greater extent with GBF1 (64%) than BIG1 (31%), whereas clathrin showed limited overlap with BIG1, and virtually none with GBF1

Selective and Signal-dependent Recruitment of Membrane Proteins to Secretory Granules Formed by Heterologously Expressed von Willebrand Factor

von Willebrand factor (vWF) is a large, multimeric protein secreted by endothelial cells and involved in hemostasis. When expressed in AtT-20 cells, vWF leads to the de novo formation of cigar-shaped organelles similar in appearance to the Weibel-Palade bodies of endothelial cells in which vWF is normally stored before regulated secretion. The membranes of this vWF-induced organelle, termed the pseudogranule, are uncharacterized. We have examined the ability of these pseudogranules, which we show are secretagogue responsive, to recruit membrane proteins. Coexpression experiments show that the Weibel-Palade body proteins P-selectin and CD63, as well as the secretory organelle membrane proteins vesicle-associated membrane protein-2 and synaptotagmin I are diverted away from the endogenous adrenocorticotropic hormone-containing secretory granules to the vWF-containing pseudogranules. However, transferrin receptor, lysosomal-associated membrane protein 1, and sialyl transferase are not recruited. The recruitment of P-selectin is dependent on a tyrosine-based motif within its cytoplasmic domain. Our data show that vWF pseudogranules specifically recruit a subset of membrane proteins, and that in a process explicitly driven by the pseudogranule content (i.e., vWF), the active recruitment of at least one component of the pseudogranule membrane (i.e., P-selectin) is dependent on residues of P-selectin that are cytosolic and therefore unable to directly interact with vWF