Cyk3 acts in actomyosin ring independent cytokinesis by recruiting Inn1 to the yeast bud neck

Cytokinesis in yeast can be achieved by plasma membrane ingression, which is dependent on actomyosin ring constriction. Inn1 presumably couples these processes by interaction with both the plasma membrane and the temporary actomyosin ring component Hof1. In addition, an actomyosin ring independent c...

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Published inMolecular genetics and genomics : MGG Vol. 282; no. 4; pp. 437 - 451
Main Authors Jendretzki, Arne, Ciklic, Ivan, Rodicio, Rosaura, Schmitz, Hans-Peter, Heinisch, Jürgen J.
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer-Verlag 01.10.2009
Springer Nature B.V
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Abstract Cytokinesis in yeast can be achieved by plasma membrane ingression, which is dependent on actomyosin ring constriction. Inn1 presumably couples these processes by interaction with both the plasma membrane and the temporary actomyosin ring component Hof1. In addition, an actomyosin ring independent cytokinesis pathway exists in yeast. We here identified Cyk3, a key component of the alternative pathway, as a novel interaction partner of Inn1. The carboxy-terminal proline rich part of Inn1 binds the SH3 domains of either Cyk3 or Hof1. Strains with truncated proteins lacking either of these SH3 domains do not display any severe phenotypes, but are synthetically lethal, demonstrating their crucial role in cytokinesis. Overexpression of CYK3 leads to an actomyosin ring independent recruitment of Inn1 to the bud neck, further supporting the significance of this interaction in vivo. Moreover, overexpression of CYK3 in a myo1 or an iqg1 deletion not only restores viability, but also the recruitment of Inn1 to the bud neck. We propose that Cyk3 is part of an actomyosin ring independent cytokinesis pathway, which acts as a rescue mechanism to recruit Inn1 to the bud neck.
AbstractList Cytokinesis in yeast can be achieved by plasma membrane ingression, which is dependent on actomyosin ring constriction. Inn1 presumably couples these processes by interaction with both the plasma membrane and the temporary actomyosin ring component Hof1. In addition, an actomyosin ring independent cytokinesis pathway exists in yeast. We here identified Cyk3, a key component of the alternative pathway, as a novel interaction partner of Inn1. The carboxy-terminal proline rich part of Inn1 binds the SH3 domains of either Cyk3 or Hof1. Strains with truncated proteins lacking either of these SH3 domains do not display any severe phenotypes, but are synthetically lethal, demonstrating their crucial role in cytokinesis. Overexpression of CYK3 leads to an actomyosin ring independent recruitment of Inn1 to the bud neck, further supporting the significance of this interaction in vivo. Moreover, overexpression of CYK3 in a myo1 or an iqg1 deletion not only restores viability, but also the recruitment of Inn1 to the bud neck. We propose that Cyk3 is part of an actomyosin ring independent cytokinesis pathway, which acts as a rescue mechanism to recruit Inn1 to the bud neck.
Cytokinesis in yeast can be achieved by plasma membrane ingression, which is dependent on actomyosin ring constriction. Inn1 presumably couples these processes by interaction with both the plasma membrane and the temporary actomyosin ring component Hof1. In addition, an actomyosin ring independent cytokinesis pathway exists in yeast. We here identified Cyk3, a key component of the alternative pathway, as a novel interaction partner of Inn1. The carboxy-terminal proline rich part of Inn1 binds the SH3 domains of either Cyk3 or Hof1. Strains with truncated proteins lacking either of these SH3 domains do not display any severe phenotypes, but are synthetically lethal, demonstrating their crucial role in cytokinesis. Overexpression of CYK3 leads to an actomyosin ring independent recruitment of Inn1 to the bud neck, further supporting the significance of this interaction in vivo. Moreover, overexpression of CYK3 in a myo1 or an iqg1 deletion not only restores viability, but also the recruitment of Inn1 to the bud neck. We propose that Cyk3 is part of an actomyosin ring independent cytokinesis pathway, which acts as a rescue mechanism to recruit Inn1 to the bud neck.
Cytokinesis in yeast can be achieved by plasma membrane ingression, which is dependent on actomyosin ring constriction. Inn1 presumably couples these processes by interaction with both the plasma membrane and the temporary actomyosin ring component Hof1. In addition, an actomyosin ring independent cytokinesis pathway exists in yeast. We here identified Cyk3, a key component of the alternative pathway, as a novel interaction partner of Inn1. The carboxy-terminal proline rich part of Inn1 binds the SH3 domains of either Cyk3 or Hof1. Strains with truncated proteins lacking either of these SH3 domains do not display any severe phenotypes, but are synthetically lethal, demonstrating their crucial role in cytokinesis. Overexpression of CYK3 leads to an actomyosin ring independent recruitment of Inn1 to the bud neck, further supporting the significance of this interaction invivo. Moreover, overexpression of CYK3 in a myo1 or an iqg1 deletion not only restores viability, but also the recruitment of Inn1 to the bud neck. We propose that Cyk3 is part of an actomyosin ring independent cytokinesis pathway, which acts as a rescue mechanism to recruit Inn1 to the bud neck.
Author Jendretzki, Arne
Ciklic, Ivan
Schmitz, Hans-Peter
Heinisch, Jürgen J.
Rodicio, Rosaura
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  fullname: Rodicio, Rosaura
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/19707790$$D View this record in MEDLINE/PubMed
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Keywords Hof1
Iqg1
Actomyosin ring
Myo1
Inn1
Cytokinesis
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PublicationTitle Molecular genetics and genomics : MGG
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Springer Nature B.V
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  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/30.6.e23
  contributor:
    fullname: U Gueldener
– volume: 144
  start-page: 1425
  year: 1996
  ident: 476_CR13
  publication-title: Genetics
  doi: 10.1093/genetics/144.4.1425
  contributor:
    fullname: P James
SSID ssj0017627
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Snippet Cytokinesis in yeast can be achieved by plasma membrane ingression, which is dependent on actomyosin ring constriction. Inn1 presumably couples these processes...
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SubjectTerms Actomyosin - metabolism
Actomyosin - physiology
Amino Acid Sequence
Animal Genetics and Genomics
Biochemistry
Biomedical and Life Sciences
Cell Cycle Proteins - metabolism
Cell division
Cytokinesis - genetics
Cytokinesis - physiology
Genomics
Human Genetics
Life Sciences
Microbial Genetics and Genomics
Microtubule-Associated Proteins - chemistry
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Microtubule-Associated Proteins - physiology
Molecular Sequence Data
Organisms, Genetically Modified
Original Paper
Phylogeny
Plant Genetics and Genomics
Plasma
Protein Binding
Protein Structure, Tertiary - physiology
Protein Transport
Proteins
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - physiology
Sequence Homology, Amino Acid
Tissue Distribution
Transfection
Yeast
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Title Cyk3 acts in actomyosin ring independent cytokinesis by recruiting Inn1 to the yeast bud neck
URI https://link.springer.com/article/10.1007/s00438-009-0476-0
https://www.ncbi.nlm.nih.gov/pubmed/19707790
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Volume 282
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