• Title/Summary/Keyword: spin

Search Result 3,838, Processing Time 0.036 seconds

Emission of spin-polarized light in GaN-based spin LEDs (GaN계 스핀 발광소자의 스핀편극된 빛의 발광)

  • Ham, Moon-Ho;Yoon, Suk-Ho;Park, Yong-Jo;Myoung, Jae-Min
    • Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
    • /
    • 2005.05a
    • /
    • pp.150-152
    • /
    • 2005

  • We investigated the fabrication and characteristics of spin-polarized LEDs based on GaN using (Ga,Mn)N as spin injection source. (Ga,Mn)N thin films were found to exhibit the ferromagnetic ordering above room temperature and the negative MR up to room temperature. The electrical characteristics in spin LEDs did not degraded in spite of the insertion of (Ga,Mn)N films. In EL spectra of spin LEDs, it is confirmed that spin LEDs emit the strong light at 7 K as well as room temperature. These results suggest that it is possible to emit spin-polarized light in our spin LEDs.

  • PDF

Regulation of SPIN90 by Cell Adhesion and ERK Activation

  • Kim Sung Hyun;Kim Dae Joong;Song Woo Keun
    • Proceedings of the Microbiological Society of Korea Conference
    • /
    • 2004.05a
    • /
    • pp.141-146
    • /
    • 2004

  • SPIN90 was identified to farm molecular complex with $\betaPIX$, WASP and Nck. This complex shows that SPIN90 interacts with Nck in a manner dependent upon cell adhesion to extracellular matrix, but $SPIN90{\cdot}{\beta}PIX{\cdot}WASP$ complex was stable even in suspended cells. This suggests that SPIN90 serves as an adaptor molecule to recruit other proteins to Nck at focal adhesions. SPIN90 was phosphorylated by ERK1, which was, itself, activated by cell adhesion and platelet-derived growth factor. Such phosphorylation of SPIN90 likely promotes the interaction of the $SPIN90{\cdot}{\beta}PIX{\cdot}WASP$ complex and Nck. It thus appears that the interaction of the $SPIN90{\cdot}{\beta}PIX{\cdot}WASP$ complex with Nck is crucial for stable cell adhesion and can be dynamically modulated by SPIN90 phosphorylation that is dependent on cell adhesion and ERX activation. SPIN90 directly binds syndapin I, syndapin isoform II-1 and II-s via its PRD region in vitro, in vivo and also associates with endocytosis core components such as clathrin and dynamin. In neuron and fibroblast, SPIN90 colocalizes with syndapins as puntate form, consistent with a role for SPIN90 in clathrin-mediated endocytosis pathway. Overexpression of SPIN90 N-term inhibits receptor-mediated endocytosis. Interestingly, SPIN90 PRD, binding interface of syndapin, significantly blocks internalization of transferrin, demonstrating SPIN90 involvement in endocytosis in vivo by interacting syndapin. Depletion of endogenous SPIN90 by introducing $\alpha-SPIN90$ also blocks receptor-mediated endocytosis. Actin polymerization could generate farce facilitating the pinch-out event in endocytosis, detach newly formed endocytic vesicle from the plasma membrane or push out them via the cytosol on actin tails. Here we found that SPIN90 localizes to high actin turn over cortical area, actin-membrane interface and membrane ruffle in PDGF treated cells. Overexpression of SPIN90 has an effect on cortical actin rearrangement as filopodia induction and it is mediated by the Arp2/3 complex at cell periphery. Consistent with a role in actin organization, CFP-SPIN90 present in actin comet tail generated by PIP5 $kinase\gamma$ overexpression. Therefore this study suggests that SPIN90 is functional linker between endocytosis and actin cytoskeleton.

  • PDF