Wu Lab

50. Yanfang Ye, Aysha H. Osmani, Zhen-Ru Liu, Addie Kern, and Jian-Qiu Wu. 2025. Fission yeast GPI inositol deacylase Bst1 regulates ER-Golgi transport and functions in late stages of cytokinesis. Mol. Biol. Cell. In press.

49. Singh D, Liu Y, Zhu YH, Zhang S, Naegele S, Wu JQ. 2024. Septins function in exocytosis via physical interactions with the exocyst complex in fission yeast cytokinesis. eLife. September 4, 2024. PMID:39026698.

48. Larissa V. G. Longo, Evelyn G. Goodyear , Sha Zhang , Elena Kudryashova , Jian-Qiu Wu. 2022. Involvement of Smi1 in cell wall integrity and glucan synthase Bgs4 localization during fission yeast cytokinesis. Mol. Biol. Cell. Feb 1;33(2):ar17. PMID: 34910579.

47. Gerien K.S., Zhang S., Russell A.C., Zhu Y.-H., Purde V., Wu J.-Q. 2020. Roles of Mso1 and the SM protein Sec1 in efficient vesicle fusion during fission yeast cytokinesis. Mol. Biol. Cell. 2020 May 20:mbcE20010067. doi: 10.1091/mbc.E20-01-0067. Online ahead of print. PMID: 32432970.

46. Lucas B.E., McPherson M.T., Hawk T.M., Wilson L.N., Kroh J.M., Hickman K.G., Fitzgerald S.R., Disbennett W.M., Rollins P.D., Hylton H.M., Baseer M.A., Montgomery P.N., Wu J.-Q., Petreaca R.C. 2019. An Assay to Study Intra-Chromosomal Deletions in Yeast. Methods Protoc. 2(3):74. PMID: 31454903.

45. Okada H. *, Wloka C. *, Wu J.-Q., Bi E. 2019. Distinct roles of myosin-II isoforms in cytokinesis under normal and stressed conditions. iScience. 14:69-87. *Co-first authors. https://www.ncbi.nlm.nih.gov/pubmed/30928696

44. Liu, Y. *, N. A. McDonald*, S.M. Naegele, K.L. Gould, and J.-Q. Wu. 2019. The F-BAR domain of Rga7 relies on a cooperative mechanism of membrane binding with a partner protein during fission yeast cytokinesis. Cell Reports. 26:2540-2548. *Co-first authors. https://www.ncbi.nlm.nih.gov/pubmed/30840879

43. Liu X.M., Yamasaki A., Du X.M., Coffman V.C., Ohsumi Y., Nakatogawa H., Wu J.-Q., Noda N.N., Du L.-L. 2018. Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein. eLIFE. 7:e41237.

42. Gerien K.S., J.-Q. Wu. 2018. Molecular mechanisms of contractile-ring constriction and membrane trafficking in cytokinesis. Biophys Rev. 10:1649-1666.

41. Zhu, Y.-H., J. Hyun, Y.-Z. Pan, J.E. Hopper, J. Rizo, J.-Q. Wu. 2018. Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis. Mol. Biol. Cell. 29:2259-2279.

40. Davidson R., J.A. Pontasch, J.-Q. Wu. 2016. Sbg1 is a novel regulator for the localization of the β-glucan synthase Bgs1 in fission yeast. PLoS One. 11: e0167043. https://www.ncbi.nlm.nih.gov/pubmed/27898700

39. Liu Y. and J.-Q. Wu. 2016. Cytokinesis: Going super resolution in live cells. Current Biology. 26:R1150-R1152. http://www.cell.com/current-biology/fulltext/S0960-9822(16)31076-4

38. Liu Y, I-J. Lee, M. Sun, C.A. Lower, K.W. Runge, J. Ma, J.-Q. Wu. 2016. Roles of the novel coiled-coil protein Rng10 in septum formation during fission yeast cytokinesis. Mol. Biol. Cell. 27:2528-2541. https://www.ncbi.nlm.nih.gov/pubmed/27385337

37. Wang, N., I-J. Lee, G. Rask, and J.-Q. Wu*. 2016. Roles of the TRAPP-II complex and the exocyst in membrane deposition during fission yeast cytokinesis. PLoS Biology 14:e1002437. http://www.ncbi.nlm.nih.gov/pubmed/27082518

36. Davidson R., Y. Liu, K.S. Gerien, and J.-Q. Wu*. 2016. Real-time visualization and quantification of contractile ring proteins in single living cells. Mothods in Mol. Biol. 1369:9-23. http://www.ncbi.nlm.nih.gov/pubmed/26519302

35. Sun, L., R. Guan, I-J. Lee, Y. Liu, M. Chen, J. Wang, J.-Q. Wu, Z. Chen. 2015. Mechanistic insights into the anchorage of the contractile ring by anillin and Mid1. Developmental Cell. 33:413-426. http://www.ncbi.nlm.nih.gov/pubmed/25959226

34. Xu, T., D. Vavylonis, F.-C. Tsai, G. Koenderink, W. Nie, E. Yusuf, I-J. Lee, J.-Q. Wu, and X. Huang. 2015. SOAX: A software for quantification of 3D biopolymer networks. Scientific Reports 5:9081. http://www.ncbi.nlm.nih.gov/pubmed/25765313

33. Davidson, R., D. Laporte, and J.-Q. Wu*. 2015. Regulation of Rho GEF Rgf3 by ­the arrestin Art1 in fission yeast cytokinesis. Mol. Biol. Cell. 26:453-466. PMCID: PMC4310737. http://www.ncbi.nlm.nih.gov/pubmed/25473118

32. Wang, N., M. Wang, Y.-H. Zhu, T.W. Grosel, D. Sun, D.S. Kudryashov, and J.-Q. Wu*. 2015. The Rho-GEF Gef3 interacts with the septin complex and activates the GTPase Rho4 during fission yeast cytokinesis. Mol. Biol. Cell. 26:238-255. http://www.ncbi.nlm.nih.gov/pubmed/25411334
[The paper has been chosen by the MBoC Editorial Board for Highlights. It appeared in the ASCB Newsletter and was considered for the MBoC Paper of the Year award.]

31. Coffman, V.C., I-J. Lee, and J.-Q. Wu*. 2014. Counting molecules within cells. Colloquium Series on Quantitative Cell Biology (e-book series). Biota Publishing, ISBN# 9781615046553.http://books.google.com/books?id=hfK9BAAAQBAJ

30. Wang, N., L. Lo Presti, Y.-H. Zhu, M. Kang, Z. Wu, S.G. Martin, and J.-Q. Wu*. 2014. The novel proteins Rng8 and Rng9 regulate the myosin-V Myo51 during fission yeast cytokinesis. J. Cell Biol. 205:357-375. http://www.ncbi.nlm.nih.gov/pubmed/24798735
[Highlighted by JCB at http://jcb.rupress.org/content/205/3/284.2.full].

29. Lee, I-J., N. Wang, W. Hu, K. Schott, J. Bähler, T.H. Giddings, Jr., J.R. Pringle, L.-L. Du, J.-Q. Wu*. 2014. Regulation of spindle-pole body assembly and cytokinesis by the centrin-binding protein Sfi1 in fission yeast. Mol. Biol. Cell. 25:2735-2749.
http://www.ncbi.nlm.nih.gov/pubmed/25031431

28. Deng, L, R. Kabeche, N. Wang, J.-Q. Wu, J.B. Moseley. 2014. Megadalton node assembly by binding of Skb1 to the membrane anchor Slf1. Mol. Biol. Cell. 25:2660-2668. http://www.ncbi.nlm.nih.gov/pubmed/25009287

27. Coffman, V.C*. and J.-Q. Wu*. 2014. Every laboratory with a fluorescence microscope should consider counting molecules. Mol. Biol. Cell. 25:1545-1548. Review.
http://www.ncbi.nlm.nih.gov/pubmed/24825827

26. Zhu, Y.-H. and J.-Q. Wu*. 2014. Cell-size control – complicated. Cell Cycle. 13:693-694. http://www.ncbi.nlm.nih.gov/pubmed/24526119

25. Coffman V.C., J.A. Sees, D.R. Kovar, and J.-Q. Wu*. 2013. The formins Cdc12 and For3 cooperate during contractile ring assembly in cytokinesis. J. Cell Biol. 203:101-114. http://www.ncbi.nlm.nih.gov/pubmed/24127216 [Highlighted by J. Cell Biology "In Focus" in 2013 at http://jcb.rupress.org/content/203/1/3.full].

24. Zhu Y.-H., Y.F. Ye, Z. Wu, and J.-Q. Wu*. 2013. Cooperation between Rho-GEF Gef2 and its binding partner Nod1 in the regulation of fission yeast cytokinesis. Mol. Biol. Cell. 24:3187-3204. http://www.ncbi.nlm.nih.gov/pubmed/23966468

23. Coffman, V.C. and J.-Q. Wu. 2012. Counting protein molecules using quantitative fluorescence microscopy. Trends in Biochemical Sciences. 37:499-506. http://www.ncbi.nlm.nih.gov/pubmed/22948030

22. Lee, I-J., V.C. Coffman and J.-Q. Wu. 2012. Contractile-ring assembly in fission yeast cytokinesis: recent advances and new perspectives. Cytoskeleton. 69:751-763. http://www.ncbi.nlm.nih.gov/pubmed/22887981

21. Laporte, D., N. Ojkic, D. Vavylonis, J.-Q. Wu. 2012. Alpha-Actinin and fimbrin cooperate with myosin II to organize actomyosin bundles during contractile-ring assembly. Mol. Biol. Cell. 23:3094-3110. http://www.ncbi.nlm.nih.gov/pubmed/22740629

20. Lee, I-J. and J.-Q. Wu. 2012. Characterization of Mid1 domains for targeting and scaffolding in fission yeast cytokinesis. J. Cell Sci. 125:2973-2985. http://www.ncbi.nlm.nih.gov/pubmed/22427686

19. Y.F. Ye, I-J. Lee, K.W. Runge, and J.-Q. Wu. 2012. Roles of putative Rho-GEF Gef2 in division-site positioning and contractile-ring function in fission yeast cytokinesis. Mol. Biol. Cell. 23:1181-1195. http://www.ncbi.nlm.nih.gov/pubmed/22298427

18. Valerie C. Coffman, P. Wu, M. Parthun, and J.-Q. Wu. 2011. CENP-A exceeds microtubule attachment sites in centromere clusters of both budding and fission yeast. J. Cell Biol. 195:563-572.
[Highlighted by JCB In Focus at: http://jcb.rupress.org/content/195/4/539.full].

17. P. Wu, R. Zhao, Y. Ye, and J.-Q. Wu. 2011. Roles of the DYRK kinase Pom2 in cytokinesis, mitochondrial morphology, and sporulation in fission yeast. PLoS ONE 6(12): e28000. doi:10.1371/journal.pone.0028000. http://www.ncbi.nlm.nih.gov/pubmed/22174761

16. Ojkic N., J.-Q. Wu., Vavylonis D. 2011. Model of myosin node aggregation into a contractile ring: the effect of local alignment. J. Phys Condens Matter 23:374103. http://iopscience.iop.org/0953-8984/23/37/374103/.

15. Laporte, D., V.C. Coffman, I-J. Lee, and J.-Q. Wu. 2011. Assembly and architecture of precursor nodes during fission yeast cytokinesis. J. Cell Biol. 192:1005-1021.
[Highlighted by JCB at: http://jcb.rupress.org/content/192/6/902.2.full].

14. Wu, J.-Q., Y.F. Ye, N. Wang, T.D. Pollard, and J.R. Pringle. 2010. Cooperation between the septins and the actomyosin ring and role of a cell-integrity pathway during cell division in fission yeast. Genetics. 186:897-915.
http://www.ncbi.nlm.nih.gov/pubmed/20739711.

13. Laporte, D., R. Zhao, and J.-Q. Wu. 2010. Mechanisms of contractile-ring assembly in fission yeast and beyond. Seminars in Cell & Dev. Biol. 21:892-898.
http://www.ncbi.nlm.nih.gov/pubmed/20708088

12. Onishi, M., T. Koga, A. Hirata, T. Nakamura, H. Asakawa, C. Shimoda, J. Bähler, J.-Q. Wu, K. Takegawa, H. Tachikawa, J.R. Pringle, Y. Fukui. 2010. Role of septins in the orientation of forespore-membrane extension during sporulation in fission yeast. Mol. Cell Biol. 30:2057-2074. http://www.ncbi.nlm.nih.gov/pubmed/20123972

11. Thomas D. Pollard and Jian-Qiu Wu. 2010. Understanding cytokinesis: lessons from fission yeast. Nature Reviews Molecular Cell Biology. 11:149-155.
http://www.nature.com/nrm/journal/v11/n2/abs/nrm2834.html.

10. Valerie C. Coffman, Aaron H. Nile, I-Ju Lee, Huayang Liu, and Jian-Qiu Wu. 2009. Roles of formin nodes and myosin motor activity in Mid1p-dependent contractile ring assembly during fission yeast cytokinesis. Mol. Biol. Cell. 20:5195-5210.
http://www.molbiolcell.org/cgi/content/full/20/24/5195.
[Highlighted in MBoC InCytes and ASCB Newsletter. ]

9. Vavylonis*, D, J.-Q. Wu*, S. Hao, B. O’Shaughnesy and T.D. Pollard. 2008. Assembly mechanism of the contractile ring for cytokinesis by fission yeast. Science 319:97-100.
*Co-first authors.
http://www.sciencemag.org/cgi/content/full/319/5859/97

8. Wu, J.-Q., C. McCormick, and T. D. Pollard. 2008. Counting proteins in living cells by quantitative fluorescence microscopy with internal standards. Methods in Cell Biol. 89:253-273. http://www.ncbi.nlm.nih.gov/pubmed/19118678

7. Wu, J.-Q., V. Sirotkin, D.K. Kovar, M. Lord, C.C. Beltzner, J.R. Kuhn, and T.D. Pollard. 2006. Assembly of the cytokinetic contractile ring from a broad band of nodes in fission yeast. J. Cell Biol. 174:391-402.
http://www.jcb.org/cgi/content/full/174/3/391

6. Wu, J.-Q. and T.D. Pollard. 2005. Counting cytokinesis proteins globally and locally in fission yeast. Science 310:310-314. http://www.sciencemag.org/cgi/content/full/310/5746/310

5. Kovar, D.R., J.-Q. Wu, and T.D. Pollard. 2005. Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast. Mol. Biol. Cell 16:2313-2324.
http://www.molbiolcell.org/cgi/content/full/16/5/2313

4. Wu, J.-Q., J.R. Kuhn, D.R. Kovar, and T.D. Pollard. 2003. Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis. Dev. Cell 5:723-734.
http://www.ncbi.nlm.nih.gov/pubmed/14602073

3. Wu, J.-Q., J. Bähler, and J.R. Pringle. 2001. Roles of a fimbrin and an a-actinin-like protein in fission yeast cell polarization and cytokinesis. Mol. Biol. Cell 12:1061-1077.
http://www.molbiolcell.org/cgi/content/full/12/4/1061

2. Hales, K.G., E. Bi, J.-Q. Wu, J.C. Adam, I.-C. Yu, and J.R. Pringle. 1999. Cytokinesis: an emerging unified theory for eukaryotes? Curr. Opin. Cell Biol. 11:717-725
http://www.ncbi.nlm.nih.gov/pubmed/?term=Cytokinesis%3A+an+emerging+unified+theory+for+eukaryotes%3F

1. Bähler, J.*, J.-Q. Wu*, M.S. Longtine, N.G. Shah, A. McKenzie III, A.B. Steever, A. Wach, P. Philippsen, and J.R. Pringle. 1998. Heterologous modules for efficient and versatile gene targeting in Schizosaccharomyces pombe. Yeast 14:943-951.
*Co-first authors
http://www3.interscience.wiley.com/cgi-bin/abstract/3913/ABSTRACT?CRETRY=1&SRETRY=0