Deep Chandra Observations of the Pulsar Wind Nebula Created by PSR B0355+54

We report on Chandra X-ray Observatory (CXO) observations of the pulsar wind nebula (PWN) associated with PSR B0355+54 (eight observations with a 395 ks total exposure, performed over an 8 month period). We investigated the spatial and spectral properties of the emission coincident with the pulsar, compact nebula (CN), and extended tail. We find that the CN morphology can be interpreted in a way that suggests a small angle between the pulsar spin axis and our line-of-sight, as inferred from the radio data. On larger scales, emission from the 7' (2 pc) tail is clearly seen. We also found hints of two faint extensions nearly orthogonal to the direction of the pulsar's proper motion. The spectrum extracted at the pulsar position can be described with an absorbed power-law + blackbody model. The nonthermal component can be attributed to magnetospheric emission, while the thermal component can be attributed to emission from either a hot spot (e.g., a polar cap) or the entire neutron star surface. Surprisingly, the spectrum of the tail shows only a slight hint of cooling with increasing distance from the pulsar. This implies either a low magnetic field with fast flow speed, or particle re-acceleration within the tail. We estimate physical properties of the PWN and compare the morphologies of the CN and the extended tail with those of other bow shock PWNe observed with long CXO exposures.Comment: 11 pages, 8 figure

Regulation of ubiquitin-binding proteins by monoubiquitination

Proteins containing ubiquitin-binding domains (UBDs) interact with ubiquitinated targets and regulate diverse biological processes, including endocytosis, signal transduction, transcription and DNA repair. Many of the UBD-containing proteins are also themselves monoubiquitinated, but the functional role and the mechanisms that underlie this modification are less well understood. Here, we demonstrate that monoubiquitination of the endocytic proteins Sts1, Sts2, Eps15 and Hrs results in intramolecular interactions between ubiquitin and their UBDs, thereby preventing them from binding in trans to ubiquitinated targets. Permanent monoubiquitination of these proteins, mimicked by the fusion of ubiquitin to their carboxyl termini, impairs their ability to regulate trafficking of ubiquitinated receptors. Moreover, we mapped the in vivo monoubiquitination site in Sts2 and demonstrated that its mutation enhances the Sts2-mediated effects of epidermal-growth-factor-receptor downregulation. We propose that monoubiquitination of ubiquitin-binding proteins inhibits their capacity to bind to and control the functions of ubiquitinated targets in vivo.