Quantitative cell biology; Cell polarity; Membrane dynamics and remodeling; ER-organelle contacts; Lipid homeostasis; Calcium signalling
Membrane-bound organelles establish multiple membrane contact sites (MCSs) through which they communicate and coordinate their functions. The broad goal of our lab is to elucidate the nature and functions of endomembrane contacts, and to integrate their roles into a general framework of cell physiology, using the fission yeast Schizosaccharomyces pombe as the main model organism.
Formation of ER/PM contacts
The endoplasmic reticulum (ER)-plasma membrane (PM) contact sites are thought to function in lipid trafficking and calcium signalling and are particularly prominent in yeast, plants and excitable cells in metazoans. A group of evolutionary conserved membrane integral proteins have been recently identified to couple the ER and the PM in various model systems. However, underlying mechanisms of the ER/PM contact formation remain poorly understood. We aim to understand mechanistically how these and potentially other proteins function in tethering the ER to the PM.
Physiological functions of ER/PM contacts
The mechanistic roles of the ER/PM contacts in calcium and lipid homeostasis, as well as their potential involvement in the PM patterning and cell stress response, require further investigation. Another main research interest is to explore the physiological consequences of establishing the ER/PM contacts.
Cell polarity and morphogenesis
Spatial coordination between endocytosis and exocytosis is essential to ensure the polarized growth and cylindrical cell shape of fission yeast cells. Specialized PM compartments at the growing ends are crucial for vesicle targeting, docking and fusion, and hence the polarized growth. We are also keen in understanding how the PM-vesicle crosstalk involves in polarity and shape maintenance of the fission yeast cells.
(*Corresponding author; #Equal contribution)
- Ng AYE.#, Ng AQE.# and Zhang D.* 2018. ER-PM contacts restrict exocytic sites for polarized morphogenesis. Current Biology 28: 146-153.e6.
- Zhang D.*, Bidone T. and Vavylonis D.* 2016. ER-PM contacts define actomyosin kinetics for proper contractile ring assembly. Current Biology 26: 647-653.
- Zhang D.* and Oliferenko S.* 2014. Tts1, the fission yeast homolog of TMEM33 family, functions in NE remodeling during mitosis. Molecular Biology of the Cell 25: 2970-2983. (Highlighted article in “Highlights from MBoC”)
- Vjestica A.#, Zhang D.#, Liu JH and Oliferenko S. 2013. Hsp70-Hsp40 chaperone complex functions in controlling polarized growth by repressing Hsf1-Driven heat stress-associated transcription. PLoS Genetics 9: e1003886. (Recommended by F1000 https://f1000.com/prime/718151387)
- Zhang D. and Oliferenko S. 2013. Remodeling the nuclear membrane in mitosis. Current Opinions in Cell Biology 25:142-8. (Invited review)
- Zhang D.#, Vjestica A.# and Oliferenko S. 2012. Plasma membrane tethering of the cortical ER necessitates its finely reticulated architecture. Current Biology 22: 2048–2052.
- Yam C., He Y.#, Zhang D.#, Chiam K. and Oliferenko S. 2011. Divergent strategies for controlling the nuclear membrane satisfy geometric constraints during nuclear division. Current Biology 21: 1314-1319.
- Zhang D., Vjestica A. and Oliferenko S. 2010. The cortical ER network limits the permissive zone for actomyosin ring assembly. Current Biology 20: 1029-1034. (Highlighted by “Dispatches” in Current Biology 20: R484-6, 2010)