Patient-on-Staff Assaults: Perspectives of Mental Health Staff at an Acute Inpatient Psychiatric Teaching Hospital in the United States.

Introduction: Physical assaults perpetrated by patients in psychiatric hospitals against mental health staff (MHS) is a serious concern facing psychiatric hospitals. Assaulted staff reports physical and psychological trauma that affects their personal and professional lives. There is a dearth of literature exploring this phenomenon.

Ploidy reduction in Saccharomyces cerevisiae.

Large-scale transitions in genome size from tetraploid to diploid were observed during a previous 1800-generation evolution experiment in Saccharomyces cerevisiae. Whether the transitions occurred via a one-step process (tetraploid to diploid) or through multiple steps (through ploidy intermediates) remained unclear. To provide insight into the mechanism involved, we investigated whether triploid-sized cells sampled from the previous experiment could also undergo ploidy loss.

PIP2 hydrolysis and calcium release are required for cytokinesis in Drosophila spermatocytes.

The role of calcium (Ca(2+)) in cytokinesis is controversial, and the precise pathways that lead to its release during cleavage are not well understood. Ca(2+) is released from intracellular stores by binding of inositol trisphosphate (IP3) to the IP3 receptor (IP3R), yet no clear role in cytokinesis has been established for the precursor of IP3, phosphatidylinositol 4,5-bisphosphate (PIP2). Here, using transgenic flies expressing PLCdelta-PH-GFP, which specifically binds PIP2, we identify PIP2 in the plasma membrane and cleavage furrows of dividing Drosophila melanogaster spermatocytes, and we establish that this phospholipid is required for continued ingression but not for initiation of cytokinesis.

Syntaxin 5 is required for cytokinesis and spermatid differentiation in Drosophila.

Syntaxin 5 is a Golgi-localized SNARE protein that has been shown to be required for ER-Golgi traffic in yeast and Golgi reassembly following cell division in mammalian cells. Here, we describe the characterization of the Drosophila ortholog of syntaxin 5, dSyx5, and show that, like its mammalian and yeast counterparts, the protein is localized to the Drosophila Golgi and binds to alpha-SNAP. Null mutations in dSyx5 are larval lethal and demonstrate impaired transport of a GFP-tagged membrane protein.