TY - JOUR
T1 - Myosin-II heavy chain and formin mediate the targeting of myosin essential light chain to the division site before and during cytokinesis
AU - Feng, Zhonghui
AU - Okada, Satoshi
AU - Cai, Guoping
AU - Zhou, Bing
AU - Bi, Erfei
N1 - Publisher Copyright:
© 2015 Feng et al.
PY - 2015/4/1
Y1 - 2015/4/1
N2 - MLC1 is a haploinsufficient gene encoding the essential light chain for Myo1, the sole myosin-II heavy chain in the budding yeast Saccharomyces cerevisiae. Mlc1 defines an essential hub that coordinates actomyosin ring function, membrane trafficking, and septum formation during cytokinesis by binding to IQGAP, myosin-II, and myosin-V. However, the mechanism of how Mlc1 is targeted to the division site during the cell cycle remains unsolved. By constructing a GFP-tagged MLC1 under its own promoter control and using quantitative live-cell imaging coupled with yeast mutants, we found that septin ring and actin filaments mediate the targeting of Mlc1 to the division site before and during cytokinesis, respectively. Both mechanisms contribute to and are collectively required for the accumulation of Mlc1 at the division site during cytokinesis. We also found that Myo1 plays a major role in the septin-dependent Mlc1 localization before cytokinesis, whereas the formin Bni1 plays a major role in the actin filament-dependent Mlc1 localization during cytokinesis. Such a two-tiered mechanism for Mlc1 localization is presumably required for the ordered assembly and robustness of cytokinesis machinery and is likely conserved across species.
AB - MLC1 is a haploinsufficient gene encoding the essential light chain for Myo1, the sole myosin-II heavy chain in the budding yeast Saccharomyces cerevisiae. Mlc1 defines an essential hub that coordinates actomyosin ring function, membrane trafficking, and septum formation during cytokinesis by binding to IQGAP, myosin-II, and myosin-V. However, the mechanism of how Mlc1 is targeted to the division site during the cell cycle remains unsolved. By constructing a GFP-tagged MLC1 under its own promoter control and using quantitative live-cell imaging coupled with yeast mutants, we found that septin ring and actin filaments mediate the targeting of Mlc1 to the division site before and during cytokinesis, respectively. Both mechanisms contribute to and are collectively required for the accumulation of Mlc1 at the division site during cytokinesis. We also found that Myo1 plays a major role in the septin-dependent Mlc1 localization before cytokinesis, whereas the formin Bni1 plays a major role in the actin filament-dependent Mlc1 localization during cytokinesis. Such a two-tiered mechanism for Mlc1 localization is presumably required for the ordered assembly and robustness of cytokinesis machinery and is likely conserved across species.
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U2 - 10.1091/mbc.E14-09-1363
DO - 10.1091/mbc.E14-09-1363
M3 - Article
C2 - 25631819
AN - SCOPUS:84926482998
VL - 26
SP - 1211
EP - 1224
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 7
ER -