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Yeast myosin light chain, Mlc1p, interacts with both IQGAP and Class II myosin to efect cytokinesis.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

  • J. R. Boyne
  • H. M. Yosuf
  • P. Biegonowski
  • C. Brenner
  • C. Price
<mark>Journal publication date</mark>15/12/2000
<mark>Journal</mark>Journal of Cell Science
Issue number24
Number of pages11
Pages (from-to)4533-4543
Publication StatusPublished
<mark>Original language</mark>English


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 G(1) and the growing bud tip during S and G(2) 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.