Majorana spintronics

We propose a systematic magnetic-flux-free approach to detect, manipulate and braid Majorana fermions in a semiconductor nanowire-based topological Josephson junction by utilizing the Majorana spin degree of freedom. We find an intrinsic $\pi$-phase difference between spin-triplet pairings enforced by the Majorana zeros modes (MZMs) at the two ends of a one-dimensional spinful topological superconductor. This $\pi$-phase is identified to be a spin-dependent superconducting phase, referred to as the spin-phase, which we show to be tunable by controlling spin-orbit coupling strength via electric gates. This electric controllable spin-phase not only affects the coupling energy between MZMs but also leads to a fractional Josephson effect in the absence of any applied magnetic flux, which enables the efficient topological qubit readout. We thus propose an all-electrically controlled superconductor-semiconductor hybrid circuit to manipulate MZMs and to detect their non-Abelian braiding statistics properties. Our work on spin properties of topological Josephson effects potentially opens up a new thrust for spintronic applications with Majorana-based semiconductor quantum circuits.Comment: 15 pages, 9 figures, replaced with published versio

Pleckstrin Homology (PH) Domain Leucine-Rich Repeat Protein Phosphatase Controls Cell Polarity by Negatively Regulating the Activity of Atypical Protein Kinase C

The proper establishment of epithelial polarity allows cells to sense and respond to signals that arise from the microenvironment in a spatiotemporally controlled manner. Atypical PKCs (aPKCs) are implicated as key regulators of epithelial polarity. However, the molecular mechanism underlying the negative regulation of aPKCs remains largely unknown. In this study, we demonstrated that PH domain leucine-rich repeat protein phosphatase (PHLPP), a novel family of Ser/Thr protein phosphatases, plays an important role in regulating epithelial polarity by controlling the phosphorylation of both aPKC isoforms. Altered expression of PHLPP1 or PHLPP2 disrupted polarization of Caco2 cells grown in 3D cell cultures as indicated by the formation of aberrant multi-lumen structures. Overexpression of PHLPP resulted in a decrease in aPKC phosphorylation at both the activation loop and the turn motif sites; conversely, knockdown of PHLPP increased aPKC phosphorylation. Moreover, in vitro dephosphorylation experiments revealed that both aPKC isoforms were substrates of PHLPP. Interestingly, knockdown of PKCζ, but not PKCι, led to similar disruption of the polarized lumen structure, suggesting that PKCζ likely controls the polarization process of Caco2 cells. Furthermore, knockdown of PHLPP altered the apical membrane localization of aPKCs and reduced the formation of aPKC-Par3 complex. Taken together, our results identify a novel role of PHLPP in regulating aPKC and cell polarity