TY - JOUR
T1 - Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis
AU - Zhu, Yi Hua
AU - Hyun, Joanne
AU - Pan, Yun Zu
AU - Hopper, James E.
AU - Rizo-Rey, Jose
AU - Wu, Jian Qiu
N1 - Funding Information:
We thank Mohan Balasubramanian, Juan Carlos, Kathy Gould, Sophie Martin, Dan Mulvihill, Beatriz Santos, Shelley Sazer, Vladimir Sirotkin, and Takashi Toda for yeast strains; Jianjie Ma and Mingzhai Sun for PALM; the Campus Microscopy and Imaging facility at OSU and the Boulder Electron Microscopy Services at the University of Colorado for help with EM; the Anita Hopper, Joseph Krzycki, Dmitri Kudryashov, and Stephen Osmani laboratories for equipment; Victoria Esser in the Rizo lab for help with liposome cofloatation assays; and the current and former members of the Wu lab and rotation student Vedud Purde for helpful suggestions and technical supports. This study was supported by a Pelotonia Graduate Fellowship to Y.-H. Z., a Pelotonia Undergraduate Fellowship to J. H., and by National Institutes of Health grants R35 NS097333 (to J.R.) and R01 GM118746 (to J.-Q.W). This work is dedicated to James E. Hopper, a caring, generous, thoughtful, outstanding mentor and colleague.
PY - 2018/9/15
Y1 - 2018/9/15
N2 - Cytokinesis is a complicated yet conserved step of the cell-division cycle that requires the coordination of multiple proteins and cellular processes. Here we describe a previously uncharacterized protein, Ync13, and its roles during fission yeast cytokinesis. Ync13 is a member of the UNC-13/Munc13 protein family, whose animal homologues are essential priming factors for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex assembly during exocytosis in various cell types, but no roles in cytokinesis have been reported. We find that Ync13 binds to lipids in vitro and dynamically localizes to the plasma membrane at cell tips during interphase and at the division site during cytokinesis. Deletion of Ync13 leads to defective septation and exocytosis, uneven distribution of cell-wall enzymes and components of cell-wall integrity pathway along the division site and massive cell lysis during cell separation. Interestingly, loss of Ync13 compromises endocytic site selection at the division plane. Collectively, we find that Ync13 has a novel function as an UNC-13/Munc13 protein in coordinating exocytosis, endocytosis, and cell-wall integrity during fission yeast cytokinesis.
AB - Cytokinesis is a complicated yet conserved step of the cell-division cycle that requires the coordination of multiple proteins and cellular processes. Here we describe a previously uncharacterized protein, Ync13, and its roles during fission yeast cytokinesis. Ync13 is a member of the UNC-13/Munc13 protein family, whose animal homologues are essential priming factors for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex assembly during exocytosis in various cell types, but no roles in cytokinesis have been reported. We find that Ync13 binds to lipids in vitro and dynamically localizes to the plasma membrane at cell tips during interphase and at the division site during cytokinesis. Deletion of Ync13 leads to defective septation and exocytosis, uneven distribution of cell-wall enzymes and components of cell-wall integrity pathway along the division site and massive cell lysis during cell separation. Interestingly, loss of Ync13 compromises endocytic site selection at the division plane. Collectively, we find that Ync13 has a novel function as an UNC-13/Munc13 protein in coordinating exocytosis, endocytosis, and cell-wall integrity during fission yeast cytokinesis.
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U2 - 10.1091/mbc.E18-04-0225
DO - 10.1091/mbc.E18-04-0225
M3 - Article
C2 - 30044717
AN - SCOPUS:85053423290
VL - 29
SP - 2259
EP - 2279
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 19
ER -