Decoherence-protected quantum gates for a hybrid solid-state spin register

Protecting the dynamics of coupled quantum systems from decoherence by the environment is a key challenge for solid-state quantum information processing. An idle qubit can be efficiently insulated from the outside world via dynamical decoupling, as has recently been demonstrated for individual solid-state qubits. However, protection of qubit coherence during a multi-qubit gate poses a non-trivial problem: in general the decoupling disrupts the inter-qubit dynamics, and hence conflicts with gate operation. This problem is particularly salient for hybrid systems, wherein different types of qubits evolve and decohere at vastly different rates. Here we present the integration of dynamical decoupling into quantum gates for a paradigmatic hybrid system, the electron-nuclear spin register. Our design harnesses the internal resonance in the coupled-spin system to resolve the conflict between gate operation and decoupling. We experimentally demonstrate these gates on a two-qubit register in diamond operating at room temperature. Quantum tomography reveals that the qubits involved in the gate operation are protected as accurately as idle qubits. We further illustrate the power of our design by executing Grover's quantum search algorithm, achieving fidelities above 90% even though the execution time exceeds the electron spin dephasing time by two orders of magnitude. Our results directly enable decoherence-protected interface gates between different types of promising solid-state qubits. Ultimately, quantum gates with integrated decoupling may enable reaching the accuracy threshold for fault-tolerant quantum information processing with solid-state devices.Comment: This is original submitted version of the paper. The revised and finalized version is in print, and is subjected to the embargo and other editorial restrictions of the Nature journa

A Membrane Fusion Protein αSNAP Is a Novel Regulator of Epithelial Apical Junctions

Tight junctions (TJs) and adherens junctions (AJs) are key determinants of the structure and permeability of epithelial barriers. Although exocytic delivery to the cell surface is crucial for junctional assembly, little is known about the mechanisms controlling TJ and AJ exocytosis. This study was aimed at investigating whether a key mediator of exocytosis, soluble N-ethylmaleimide sensitive factor (NSF) attachment protein alpha (αSNAP), regulates epithelial junctions. αSNAP was enriched at apical junctions in SK-CO15 and T84 colonic epithelial cells and in normal human intestinal mucosa. siRNA-mediated knockdown of αSNAP inhibited AJ/TJ assembly and establishment of the paracellular barrier in SK-CO15 cells, which was accompanied by a significant down-regulation of p120-catenin and E-cadherin expression. A selective depletion of p120 catenin effectively disrupted AJ and TJ structure and compromised the epithelial barrier. However, overexpression of p120 catenin did not rescue the defects of junctional structure and permeability caused by αSNAP knockdown thereby suggesting the involvement of additional mechanisms. Such mechanisms did not depend on NSF functions or induction of cell death, but were associated with disruption of the Golgi complex and down-regulation of a Golgi-associated guanidine nucleotide exchange factor, GBF1. These findings suggest novel roles for αSNAP in promoting the formation of epithelial AJs and TJs by controlling Golgi-dependent expression and trafficking of junctional proteins

CLMP Is Essential for Intestinal Development, but Does Not Play a Key Role in Cellular Processes Involved in Intestinal Epithelial Development

<p>Loss-of-function mutations in CLMP have been found in patients with Congenital Short Bowel Syndrome (CSBS), suggesting that its encoded protein plays a major role in intestinal development. CLMP is a membrane protein that co-localizes with tight junction proteins, but its function is largely unknown. We expressed wild-type (WT)-CLMP and a mutant-CLMP (associated with CSBS) in human intestinal epithelial T84 cells that, as we show here, do not produce endogenous CLMP. We investigated the effects of WT-CLMP and mutant-CLMP proteins on key cellular processes that are important for intestinal epithelial development, including migration, proliferation, viability and transepithelial resistance. Our data showed that expression of WT-CLMP or mutant-CLMP does not affect any of these processes. Moreover, our aggregation assays in CHO cells show that CLMP does not act as a strong adhesion molecule. Thus, our data suggest that, in the in vitro model systems we used, the key processes involved in intestinal epithelial development appear to be unaffected by WT-CLMP or mutant-CLMP. Further research is needed to determine the role of CLMP in the development of the intestine.</p>