Explore the vast range of titles available.

Over the past several years, scholars of political behavior have become increasingly interested in the nationalization of U.S. elections. Research has shown that there is now a strong connection between presidential vote patterns and voting in House, Senate, gubernatorial, and state legislative elections. In this article, we extend previous research by examining the role of the presidential vote in state supreme court elections. Using an original dataset containing county-level election results (N = 15,237) from 2000-2018 for all states that hold partisan or nonpartisan state supreme court elections, we examine the influence of presidential vote share in state supreme court elections. A number of important findings emerge. First, we find that presidential vote share influences voting in state supreme court contests. There is a statistically significant relationship in both partisan and nonpartisan elections even after controlling for incumbency, though the relationship is much stronger in states with partisan elections. Second, the relationship between presidential vote share and the state supreme court vote has been quite stable over time in states with partisan elections. Third, in states with states with nonpartisan elections, there has been some variability in the relationship between presidential and state supreme court voting patterns, although the data reveal an uptick in the strength of the relationship over time. Future research should continue to track the role of national political forces in state supreme court elections.

Small GTPases of the Rab family not only regulate target recognition in membrane traffic but also control other cellular functions such as cytoskeletal transport and autophagy. Here we show that Rab26 is specifically associated with clusters of synaptic vesicles in neurites. Overexpression of active but not of GDP-preferring Rab26 enhances vesicle clustering, which is particularly conspicuous for the EGFP-tagged variant, resulting in a massive accumulation of synaptic vesicles in neuronal somata without altering the distribution of other organelles. Both endogenous and induced clusters co-localize with autophagy-related proteins such as Atg16L1, LC3B and Rab33B but not with other organelles. Furthermore, Atg16L1 appears to be a direct effector of Rab26 and binds Rab26 in its GTP-bound form, albeit only with low affinity. We propose that Rab26 selectively directs synaptic and secretory vesicles into preautophagosomal structures, suggesting the presence of a novel pathway for degradation of synaptic vesicles. Our brain contains billions of cells called neurons that form an extensive network through which information is readily exchanged. These cells connect to each other via junctions called synapses. Our developing brain starts off with far more synapses than it needs, but the excess synapses are destroyed as the brain matures. Even in adults, synapses are continuously made and destroyed in response to experiences and learning. Inside neurons there are tiny bubble-like compartments called vesicles that supply the synapses with many of the proteins and other components that they need. There is a growing body of evidence that suggests these vesicles are rapidly destroyed once a synapse is earmarked for destruction, but it is not clear how this may occur. Here, Binotti, Pavlos et al. found that a protein called Rab26 sits on the surface of the vesicles near synapses. This protein promotes the formation of clusters of vesicles, and a membrane sometimes surrounds these clusters. Further experiments indicate that several proteins involved in a process called autophagy—where unwanted proteins and debris are destroyed—may also be found around the clusters of vesicles. Autophagy starts with the formation of a membrane around the material that needs to be destroyed. This seals the material off from rest of the cell so that enzymes can safely break it down. Binotti, Pavlos et al. found that one of the autophagy proteins—called Atg16L—can bind directly to Rab26, but only when Rab26 is in an ‘active’ state. These findings suggest that excess vesicles at synapses may be destroyed by autophagy. Further work will be required to establish how this process is controlled and how it is involved in the loss of synapses.