Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis

J. R. Boyne, H. M. Yosuf, P. Bieganowski, C. Brenner, C. Price

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

MLC1 (myosin light chain) acts as a dosage suppressor of a temperature sensitive mutation in the gene encoding the S. cerevisiae IQGAP protein. Both proteins localize to the bud neck in mitosis although Mlc1p localisation precedes Iqg1p. Mlc1p is also found at the incipient bud site in G1 and the growing bud tip during S and G2 phases of the cell cycle. A dominant negative GST-Mlc1p fusion protein specifically blocks cytokinesis and prevents Iqg1p localisation to the bud neck, as does depletion of Mlc1p. These data support a direct interaction between the two proteins and immunoprecipitation experiments confirm this prediction. Mlc1p is also shown to interact with the class II conventional myosin (Myo1p). All three proteins form a complex, however, the interaction between Mlc1p and Iqg1p can be separated from the Mlc1p/Myo1p interaction. Mlc1p localisation and maintenance at the bud neck is independent of actin, Myo1p and Iqg1p. It is proposed that Mlc1p therefore functions to recruit Iqg1p and in turn actin to the actomyosin ring and that it is also required for Myo1p function during ring contraction.

LanguageEnglish
Pages4533-4543
Number of pages11
JournalJournal of Cell Science
Volume113
Issue number24
Publication statusPublished - 15 Dec 2000
Externally publishedYes

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Myosin Type II
Myosin Light Chains
Cytokinesis
Yeasts
Actins
Proteins
Saccharomyces cerevisiae Proteins
Actomyosin
G2 Phase
S Phase
Immunoprecipitation
Mitosis
Cell Cycle
Maintenance
Mutation
Temperature
Genes

Cite this

Boyne, J. R., Yosuf, H. M., Bieganowski, P., Brenner, C., & Price, C. (2000). Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis. Journal of Cell Science, 113(24), 4533-4543.
Boyne, J. R. ; Yosuf, H. M. ; Bieganowski, P. ; Brenner, C. ; Price, C. / Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis. In: Journal of Cell Science. 2000 ; Vol. 113, No. 24. pp. 4533-4543.
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Boyne, JR, Yosuf, HM, Bieganowski, P, Brenner, C & Price, C 2000, 'Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis', Journal of Cell Science, vol. 113, no. 24, pp. 4533-4543.

Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis. / Boyne, J. R.; Yosuf, H. M.; Bieganowski, P.; Brenner, C.; Price, C.

In: Journal of Cell Science, Vol. 113, No. 24, 15.12.2000, p. 4533-4543.

Research output: Contribution to journalArticle

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T1 - Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis

AU - Boyne, J. R.

AU - Yosuf, H. M.

AU - Bieganowski, P.

AU - Brenner, C.

AU - Price, C.

PY - 2000/12/15

Y1 - 2000/12/15

N2 - MLC1 (myosin light chain) acts as a dosage suppressor of a temperature sensitive mutation in the gene encoding the S. cerevisiae IQGAP protein. Both proteins localize to the bud neck in mitosis although Mlc1p localisation precedes Iqg1p. Mlc1p is also found at the incipient bud site in G1 and the growing bud tip during S and G2 phases of the cell cycle. A dominant negative GST-Mlc1p fusion protein specifically blocks cytokinesis and prevents Iqg1p localisation to the bud neck, as does depletion of Mlc1p. These data support a direct interaction between the two proteins and immunoprecipitation experiments confirm this prediction. Mlc1p is also shown to interact with the class II conventional myosin (Myo1p). All three proteins form a complex, however, the interaction between Mlc1p and Iqg1p can be separated from the Mlc1p/Myo1p interaction. Mlc1p localisation and maintenance at the bud neck is independent of actin, Myo1p and Iqg1p. It is proposed that Mlc1p therefore functions to recruit Iqg1p and in turn actin to the actomyosin ring and that it is also required for Myo1p function during ring contraction.

AB - MLC1 (myosin light chain) acts as a dosage suppressor of a temperature sensitive mutation in the gene encoding the S. cerevisiae IQGAP protein. Both proteins localize to the bud neck in mitosis although Mlc1p localisation precedes Iqg1p. Mlc1p is also found at the incipient bud site in G1 and the growing bud tip during S and G2 phases of the cell cycle. A dominant negative GST-Mlc1p fusion protein specifically blocks cytokinesis and prevents Iqg1p localisation to the bud neck, as does depletion of Mlc1p. These data support a direct interaction between the two proteins and immunoprecipitation experiments confirm this prediction. Mlc1p is also shown to interact with the class II conventional myosin (Myo1p). All three proteins form a complex, however, the interaction between Mlc1p and Iqg1p can be separated from the Mlc1p/Myo1p interaction. Mlc1p localisation and maintenance at the bud neck is independent of actin, Myo1p and Iqg1p. It is proposed that Mlc1p therefore functions to recruit Iqg1p and in turn actin to the actomyosin ring and that it is also required for Myo1p function during ring contraction.

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