An efficient voxelization algorithm is presented for polygonal models by using the hardware support for the 2 D rasterization algorithm and the GPU programmable function to satisfy the volumetric display system. The v...An efficient voxelization algorithm is presented for polygonal models by using the hardware support for the 2 D rasterization algorithm and the GPU programmable function to satisfy the volumetric display system. The volume is sampled into slices by the rendering hardware and then slices are rasterated into a series of voxels. A composed buffer is used to record encoded voxels of the target volume to reduce the graphic memory requirement. In the algorithm, dynamic vertexes and index buffers are used to improve the voxelization efficiency. Experimental results show that the algorithm is efficient for a true 3-D display system.展开更多
NF-κB-inducing kinase （NIK） is required for NF-κB activation based on the processing of NF-κB p100. Here we report a novel mechanism of NIK regulation involving the chaperone 90 kDa heat shock protein （Hsp90） a...NF-κB-inducing kinase （NIK） is required for NF-κB activation based on the processing of NF-κB p100. Here we report a novel mechanism of NIK regulation involving the chaperone 90 kDa heat shock protein （Hsp90） and autophagy. Functional inhibition of lisp90 by the anti-tumor agent geldanamycin （GA） efficiently disrupts its interaction with NIK, resulting in NIK degradation and subsequent blockage of p100 processing. Surprisingly, GA-induced NIK degradation is mediated by autophagy, but largely independent of the ubiquitin-proteasome system. Hsp90 seems to be specifically involved in the folding/stabilization of NIK protein, because GA inhibition does not affect NIK mRNA transcription and translation. Furthermore, Hsp90 is not required for NIK-mediated recruitment of the α subunit of IκB3 kinase to p 100, a key step in induction of p100 processing. These findings define an alternative mechanism for Hsp90 client degradation and identify a novel function ofautophagy in NF-κB regulation. These findings also suggest a new therapeutic strategy for diseases associated with p 100 processing.展开更多
In eukaryotic cells, receptor endocytosis is a key event regulating signaling transduction. Adiponectin receptors belong to a new receptor family that is distinct from G-protein-coupled receptors and has critical role...In eukaryotic cells, receptor endocytosis is a key event regulating signaling transduction. Adiponectin receptors belong to a new receptor family that is distinct from G-protein-coupled receptors and has critical roles in the pathogenesis of diabetes and metabolic syndrome. Here, we analyzed the endocytosis of adiponectin and adiponectin receptor 1 （AdipoR1） and found that they are both internalized into transferrin-positive compartments that follow similar traffic routes. Blocking clathrin-mediated endocytosis by expressing Eps15 mutants or depleting K^＋ trapped AdipoR1 at the plasma membrane, and K^＋ depletion abolished adiponectin internalization, indicating that the endocytosis of AdipoR1 and adiponectin is clathrin-dependent. Depletion of K^＋ and overexpression of Eps15 mutants enhance adiponectin- stimulated AMP-activated protein kinase phosphorylation, suggesting that the endocytosis of AdipoR1 might down-regulate adiponectin signaling. In addition, AdipoR1 colocalizes with the small GTPase Rab5, and a dominant negative Rab5 abrogates AdipoR1 endocytosis. These data indicate that AdipoR1 is internalized through a clathrin- and Rab5- dependent pathway and that endocytosis may play a role in the regulation of adiponectin signaling.展开更多
文摘An efficient voxelization algorithm is presented for polygonal models by using the hardware support for the 2 D rasterization algorithm and the GPU programmable function to satisfy the volumetric display system. The volume is sampled into slices by the rendering hardware and then slices are rasterated into a series of voxels. A composed buffer is used to record encoded voxels of the target volume to reduce the graphic memory requirement. In the algorithm, dynamic vertexes and index buffers are used to improve the voxelization efficiency. Experimental results show that the algorithm is efficient for a true 3-D display system.
文摘NF-κB-inducing kinase （NIK） is required for NF-κB activation based on the processing of NF-κB p100. Here we report a novel mechanism of NIK regulation involving the chaperone 90 kDa heat shock protein （Hsp90） and autophagy. Functional inhibition of lisp90 by the anti-tumor agent geldanamycin （GA） efficiently disrupts its interaction with NIK, resulting in NIK degradation and subsequent blockage of p100 processing. Surprisingly, GA-induced NIK degradation is mediated by autophagy, but largely independent of the ubiquitin-proteasome system. Hsp90 seems to be specifically involved in the folding/stabilization of NIK protein, because GA inhibition does not affect NIK mRNA transcription and translation. Furthermore, Hsp90 is not required for NIK-mediated recruitment of the α subunit of IκB3 kinase to p 100, a key step in induction of p100 processing. These findings define an alternative mechanism for Hsp90 client degradation and identify a novel function ofautophagy in NF-κB regulation. These findings also suggest a new therapeutic strategy for diseases associated with p 100 processing.
文摘In eukaryotic cells, receptor endocytosis is a key event regulating signaling transduction. Adiponectin receptors belong to a new receptor family that is distinct from G-protein-coupled receptors and has critical roles in the pathogenesis of diabetes and metabolic syndrome. Here, we analyzed the endocytosis of adiponectin and adiponectin receptor 1 （AdipoR1） and found that they are both internalized into transferrin-positive compartments that follow similar traffic routes. Blocking clathrin-mediated endocytosis by expressing Eps15 mutants or depleting K^＋ trapped AdipoR1 at the plasma membrane, and K^＋ depletion abolished adiponectin internalization, indicating that the endocytosis of AdipoR1 and adiponectin is clathrin-dependent. Depletion of K^＋ and overexpression of Eps15 mutants enhance adiponectin- stimulated AMP-activated protein kinase phosphorylation, suggesting that the endocytosis of AdipoR1 might down-regulate adiponectin signaling. In addition, AdipoR1 colocalizes with the small GTPase Rab5, and a dominant negative Rab5 abrogates AdipoR1 endocytosis. These data indicate that AdipoR1 is internalized through a clathrin- and Rab5- dependent pathway and that endocytosis may play a role in the regulation of adiponectin signaling.
