Systematic Mutational Analysis of the Intracellular Regions of Yeast Gap1 Permease

The yeast general amino acid permease Gap1 is a convenient model for studying the intracellular trafficking of membrane proteins. Present at the plasma membrane when the nitrogen source is poor, it undergoes ubiquitin-dependent endocytosis and degradation upon addition of a good nitrogen source, e.g. ammonium. It comprises 12 transmembrane domains (TM) flanked by cytosol-facing N- and C-terminal tails (NT, CT). The NT of Gap1 contains the acceptor lysines for ubiquitylation and its CT includes a sequence essential to exit from the endoplasmic reticulum (ER).Journal ArticleResearch Support, Non-U.S. Gov'tSCOPUS: ar.jinfo:eu-repo/semantics/publishe

Study protocol of the iMPaCT project : A longitudinal cohort study assessing psychological determinants, sexual behaviour and chlamydia (re)infections in heterosexual STI clinic visitors

Acknowledgements We are grateful to the staff at the STI clinics of Amsterdam, Kennemerland, Hollands Noorden, Twente, who are involved in the recruitment and data collection of participants, and Marlous Ratten and Klazien Visser from Soapoli-online, who are involved in the coordination of laboratory testing of the home-based sampling kits at six-month follow-up. We also thank the staff at the STI department at the National Institute for Public Health and the Environment, especially Birgit van Benthem. Funding This project is funded by the Strategic Programme (SPR) of the National Institute for Public Health and the Environment (RIVM) (project number S/113004/01/IP). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Availability of data and materials The dataset (anonymised) generated during this study will be made available for interested parties on request.Peer reviewedPublisher PD