Polycystic kidney disease channel and synaptotagmin homologues play roles in schizosaccharomyces pombe cell wall synthesis/repair and membrane protein trafficking.
Eukaryotic cells can sense a wide variety of environmental stresses, including changes in temperature, pH, osmolarity and nutrient availability. They respond to these changes through a variety of signal-transduction mechanisms, including activation of Ca(2+)-dependent signaling pathways. This research has discovered important implications in the function(s) of polycystic kidney disease (PKD) channels and the mechanisms through which they act in the control of cell growth and cell polarity in Schizosaccharomyces pombe by ion channel-mediated Ca(2+) signaling. Pkd2 was expressed maximally during the exponential growth phase. At the cell surface pkd2 was localized at the cell tip during the G(2) phase of the cell cycle, although following cell wall damage, the cell surface-expressed protein relocalized to the whole plasma membrane. Pkd2 depletion affected Golgi trafficking, resulting in a buildup of vesicles at the cell poles, and strongly affected plasma membrane protein delivery. Surface-localized pkd2 was present in the plasma membrane for a very short time and was rapidly internalized. Internalization was dependent on Ca(2+), enhanced by amphipaths and inhibited by gadolinium. The pkd2 protein was in a complex with a yeast synaptotagmin homologue and myosin V. Depletion of pkd2 severely affected the localization of glucan synthase. A role for pkd2 in a cell polarity and cell wall synthesis signaling complex with a synaptotagmin homologue, myosin V and glucan synthase is proposed.
Aydar
Ebru
E
Institute for Health Research and Policy, London Metropolitan University, 166-220 Holloway Road, London, N7 8DB, UK.
Palmer
Christopher P
CP
D015153:Blotting, Western; D002453:Cell Cycle / Q000502:physiology; D016764:Cell Polarity / Q000502:physiology*; D002473:Cell Wall / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D005964:Glucosyltransferases / Q000378:metabolism; D047468:Immunoprecipitation; D007473:Ion Channels / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D008565:Membrane Proteins / Q000378:metabolism*; D018613:Microscopy, Confocal; D024701:Myosin Type V / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D021381:Protein Transport / Q000502:physiology*; D012568:Schizosaccharomyces / Q000166:cytology / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D050857:Synaptotagmins / Q000378:metabolism
D007473:Ion Channels; D008565:Membrane Proteins; D029702:Schizosaccharomyces pombe Proteins; D050857:Synaptotagmins; D005964:Glucosyltransferases; C040232:glucan synthase; D024701:Myosin Type V