TY - JOUR
T1 - Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p
AU - Wagner, Wolfgang
AU - Bielli, Pamela
AU - Wacha, Stefan
AU - Ragnini-Wilson, Antonella
PY - 2002/12/2
Y1 - 2002/12/2
N2 - Little is known about the molecular machinery that directs secretory vesicles to the site of cell separation during cytokinesis. We show that in Saccharomyces cerevisiae, the class V myosin Myo2p and the Rab/Ypt Sec4p, that are required for vesicle polarization processes at all stages of the cell cycle, form a complex with each other and with a myosin light chain, Mlc1p, that is required for actomyosin ring assembly and cytokinesis. Mlc1p travels on secretory vesicles and forms a complex(es) with Myo2p and/or Sec4p. Its functional interaction with Myo2p is essential during cytokinesis to target secretory vesicles to fill the mother bud neck. The role of Mlc1p in actomyosin ring assembly instead is dispensable for this process. Therefore, in yeast, as recently shown in mammals, class V myosins associate with vesicles via the formation of a complex with Rab/Ypt proteins. Furthermore, myosin light chains, via their ability to be transported by secretory vesicles and to interact with class V myosin IQ motifs, can regulate vesicle polarization processes at a specific location and stage of the cell cycle.
AB - Little is known about the molecular machinery that directs secretory vesicles to the site of cell separation during cytokinesis. We show that in Saccharomyces cerevisiae, the class V myosin Myo2p and the Rab/Ypt Sec4p, that are required for vesicle polarization processes at all stages of the cell cycle, form a complex with each other and with a myosin light chain, Mlc1p, that is required for actomyosin ring assembly and cytokinesis. Mlc1p travels on secretory vesicles and forms a complex(es) with Myo2p and/or Sec4p. Its functional interaction with Myo2p is essential during cytokinesis to target secretory vesicles to fill the mother bud neck. The role of Mlc1p in actomyosin ring assembly instead is dispensable for this process. Therefore, in yeast, as recently shown in mammals, class V myosins associate with vesicles via the formation of a complex with Rab/Ypt proteins. Furthermore, myosin light chains, via their ability to be transported by secretory vesicles and to interact with class V myosin IQ motifs, can regulate vesicle polarization processes at a specific location and stage of the cell cycle.
KW - Class V myosin
KW - Cytokinesis
KW - Myosin light chain
KW - Polarized vesicle transport
KW - Rab
KW - Ypt proteins
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U2 - 10.1093/emboj/cdf650
DO - 10.1093/emboj/cdf650
M3 - Article
C2 - 12456647
AN - SCOPUS:0037011063
VL - 21
SP - 6397
EP - 6408
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 23
ER -