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Working memory (WM) has a limited capacity; however, this limitation can be mitigated by selecting individual items from the set currently held in WM for prioritization. The selection mechanism underlying this prioritization ability is referred to as the focus of attention (FOA) in WM. Although impressive progress has been achieved in recent years, a fundamental question remains unclear: Do perception and WM share one FOA? In the current study, we investigated the hypothesis that only a perceptual task tapping object-based attention can divert the FOA in WM. We adopted a retro-cue WM paradigm and inserted a perceptual task after the offset of the cue. Critically, we manipulated the type of attention (object-based attention in Experiments 1-3, feature-based attention in Experiment 4, and spatial attention in Experiment 5) consumed by the perceptual task. We found that participants were able to prioritize a retro-cued representation in WM, and the retro-cue benefit on memory accuracy was intact regardless of the perceptual task. Critically, the retro-cue benefit on the response time of WM task was significantly reduced only after an object-based attention perceptual task (Experiments 1, 2, 3a, and 3b), while remaining constant after a feature-based attention (Experiment 4) or spatial attention (Experiment 5) perceptual task. These results suggest that WM and perception share an object-based FOA, and an object-based attention perceptual task can divert the FOA in WM. Meanwhile, the current study further confirms that sustained attention is not necessary for selective maintenance in WM. [ABSTRACT FROM AUTHOR]

Chemical de-caging has emerged as an attractive strategy for gain-of-function study of proteins via small-molecule reagents. The previously reported chemical de-caging reactions have been largely centered on liberating the side chain of lysine on a given protein. Herein, we developed an allene-based caging moiety and the corresponding palladium de-caging reagents for chemical rescue of tyrosine (Tyr) activity on intracellular proteins. This bioorthogonal de-caging pair has been successfully applied to unmask enzymatic Tyr sites (e.g., Y671 on Taq polymerase and Y728 on Anthrax lethal factor) as well as the post-translational Tyr modification site (Y416 on Src kinase) in vitro and in living cells. Our strategy provides a general platform for chemical rescue of Tyr-dependent protein activity inside cells. [ABSTRACT FROM AUTHOR]