Trade in Goods Within Multinational Companies: Survey-Based Data and Findings for the United States of America

This paper discusses the data on U.S. intrafirm trade in goods collected in BEA's surveys of the operations of U.S. multinational firms and foreign-owned U.S. affiliates. It also examines patterns that emerge from the data, with a particular focus on the intrafirm-trade shares of U.S. exports and imports by major trading partner. The paper concludes with a brief overview of selected research on intrafirm trade based on BEA's data.

International Fragmentation of Production and the Intrafirm Trade of U.s. Multinational Companies

An aspect of globalization that has attracted increased attention in recent years is trade in intermediate inputs associated with the fragmentation of production across national borders. This trade takes the form of intrafirm transactions when production stages in different countries are performed by vertically integrated units of a multinational firm. Using firm-level data on U.S. multinational companies collected by the U.S. Bureau of Economic Analysis, this paper examines intrafirm shipments of intermediate inputs from U.S. parent companies to their foreign manufacturing affiliates. We relate the propensity of affiliates to source intermediate inputs from their parents to characteristics of the parent company, of the affiliate, and of the affiliate’s host country and industry that we hypothesize will influence the volume of intrafirm trade associated with fragmentation. Our results indicate that this trade is positively related to industry and affiliate characteristics that suggest fragmented production, to host-country characteristics that offer cost advantages, and to parent and affiliate characteristics that favor internalized transactions and the active coordination of different stages of the production process. The signs on the coefficients for a number of variables suggest a division of labor between higher-skilled, or more technologically advanced, activities performed by the parent and lower-skilled, or more rudimentary, activities performed by the affiliate.

Listeria's right-handed helical rocket-tail trajectories: mechanistic implications for force generation in actin-based motility

Listeria monocytogenes forms right-handed helical rocket tail trajectories during actin-based motility in cell-free extracts, and this stereochemical feature is consistent with actoclampin's affinity-modulated, clamped-filament elongation model [Dickinson and Purich, 2002: Biophys J 82:605-617]. In that mechanism, right-handed torque is generated by an end-tracking molecular motor, each comprised of a filament barbed end and clamping protein that processively traces the right-handed helix of its filament partner. By contrast, torque is not a predicted property of those models (e.g., elastic propulsion, elastic Brownian ratchet, tethered ratchet, and insertional polymerization models) requiring filament barbed ends to depart/detach from the motile object's surface during/after each monomer-addition step. Helical trajectories also explain why Listeria undergoes longitudinal-axis rotation on a length-scale matching the helical periodicity of Listeria's rocket tails

Actin-based endosome and phagosome rocketing in macrophages: activation by the secretagogue antagonists lanthanum and zinc

Although motile endocytic vesicles form actin-rich rocket tails [Merrifield et al., 1999: Nature Cell Biol 1:72-74], the mechanism of intracellular organelle locomotion remains poorly understood. We now demonstrate that bone marrow macrophages treated with lanthanum and zinc ions, well-known secretagogue antagonists, reliably exhibit vesicle motility. This treatment results in accentuated membrane ruffling and the formation of phagosomes and early endosomes that move rapidly through the cytoplasm by assembling actin filament rocket tails. Protein-specific immunolocalization demonstrated the presence of Arp2/3 complex in the polymerization zone and throughout the actin-rich tail, whereas N-WASP was most abundant in the polymerization zone. Although Arp2/3 and N-WASP play essential roles in nucleating filament assembly, other processes (i.e., elongation and filament cross-linking) are required to produce forces needed for motility. Efficient elongation was found to require zyxin, VASP, and profilin, proteins that interact by means of their ABM-1 and ABM-2 proline-rich motifs. The functional significance of these motifs was demonstrated by inhibition of vesicle motility by the motif-specific ABM-1 and ABM-2 analogues. Furthermore, lanthanum/zinc treatment also facilitated the early onset of actin-based vaccinia motility, a process that also utilizes Arp2/3 and N-WASP for nucleation and the zyxin-VASP-profilin complex for efficient elongation. Although earlier studies using cell extracts clouded the role of oligoproline sequences in activating the polymerization zone, our studies emphasize the importance of evaluating motility in living cells