Small-time fluctuations for sub-Riemannian diffusion loops

We study the small-time fluctuations for diffusion processes which are conditioned by their initial and final positions, under the assumptions that the diffusivity has a sub-Riemannian structure and that the drift vector field lies in the span of the sub-Riemannian structure. In the case where the endpoints agree and the generator of the diffusion process is non-elliptic at that point, the deterministic Malliavin covariance matrix is always degenerate. We identify, after a suitable rescaling, another limiting Malliavin covariance matrix which is non-degenerate, and we show that, with the same scaling, the diffusion Malliavin covariance matrices are uniformly non-degenerate. We further show that the suitably rescaled fluctuations of the diffusion loop converge to a limiting diffusion loop, which is equal in law to the loop we obtain by taking the limiting process of the unconditioned rescaled diffusion processes and condition it to return to its starting point. The generator of the unconditioned limiting rescaled diffusion process can be described in terms of the original generator

New insights into subcomplex assembly and modifications of centrosomal proteins

This review provides a brief overview of the recent work on centrosome proteomics, protein complex identification and functional characterization with an emphasis on the literature of the last three years. Proteomics, genetic screens and comparative genomics studies in different model organisms have almost exhaustively identified the molecular components of the centrosome. However, much knowledge is still missing on the protein-protein interactions, protein modifications and molecular changes the centrosome undergoes throughout the cell cycle and development. The dynamic nature of this large multi-protein complex is reflected in the variety of annotated subcellular locations and biological processes of its proposed components. Some centrosomal proteins and complexes have been studied intensively in different organisms and provided detailed insight into centrosome functions. For example, the molecular, structural and functional characterization of the gamma-Tubulin ring complex (gamma-TuRC) and the the discovery of the Augmin/HAUS complex has advanced our understanding of microtubule (MT) capture, nucleation and organization. Surprising findings revealed new functions and localizations of proteins that were previously regarded as bona fide centriolar or centrosome components, e.g. at the kinetochore or in the nuclear pore complex regulating MT plus end capture or mRNA processing. Many centrosome components undergo posttranslational modifications such as phosphorylation, SUMOylation and ubiquitylation that are critical in modulating centrosome function and biology. A wealth of information has recently become available driven by new developments in technologies such as mass spectrometry, light and electron microscopy providing more detailed molecular and structural definition of the centrosome and particular roles of proteins throughout the cell cycle and development

Ultra Structural Characterisation of Tetherin - a Protein Capable of Preventing Viral Release from the Plasma Membrane

Tetherin is an antiviral restriction factor made by mammalian cells to protect them from viral infection. It prevents newly formed virus particles from leaving infected cells. Its antiviral mechanism appears to be remarkably uncomplicated. In 2 studies published in PLoS Pathogens electron microscopy is used to support the hypothesis that the tethers that link HIV-1 virions to tetherin expressing cells contain tetherin and are likely to contain tetherin alone. They also show that the HIV-1 encoded tetherin antagonist that is known to cause tetherin degradation, Vpu, serves to reduce the amount of tetherin in the particles thereby allowing their release