Mip1 associates with both the Mps1 kinase and actin, and is required for cell cortex stability and anaphase spindle positioning

Christopher P. Mattison, Jason Stumpff, Linda Wordeman, Mark Winey

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The Mps1 family of protein kinases contributes to cell cycle control by regulating multiple microtubule cytoskeleton activities. We have uncovered a new Mps1 substrate that provides a novel link between Mps1 and the actin cytoskeleton. We have identified a conserved human Mps1 (hMps1) interacting protein and have termed Mps1 interacting protein-1 (Mip1). Mip1 defines an uncharacterized family of conserved proteins that contain coiled-coil and calponin homology domains. We demonstrate that Mip1 is a phosphoprotein that interacts with hMps1 in vitro and in vivo and is a hMps1 substrate. Mip1 exhibits dynamic localization during the cell cycle; Mip1 localizes to the actin cytoskeleton during interphase, the spindle in early mitosis and the cleavage furrow during cytokinesis. Mip1 function is required to ensure proper spindle positioning at the onset of anaphase after cells begin furrow ingression. Cells depleted of Mip1 exhibit aberrant mitotic actin filament organization, excessive membrane blebbing, dramatic spindle rocking and chromosome distribution errors during early cytokinesis producing high numbers of binucleate cells. our data indicate that Mip1 is a newly recognized component of the actin cytoskeleton that interacts with hMps1 and that it is essential to ensure proper segregation of the genome during cell cleavage.

Original languageEnglish (US)
Pages (from-to)783-793
Number of pages11
JournalCell Cycle
Volume10
Issue number5
DOIs
StatePublished - Mar 1 2011
Externally publishedYes

Fingerprint

Anaphase
Actin Cytoskeleton
Proteins
Cytokinesis
actin kinase
Phosphoproteins
Interphase
Blister
Cell Cycle Checkpoints
Cytoskeleton
Mitosis
Microtubules
Protein Kinases
Cell Cycle
Cell Count
Chromosomes
Genome
Membranes

Keywords

  • Actin
  • Cytokinesis
  • Mip1
  • Mps1 kinase

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

Cite this

Mip1 associates with both the Mps1 kinase and actin, and is required for cell cortex stability and anaphase spindle positioning. / Mattison, Christopher P.; Stumpff, Jason; Wordeman, Linda; Winey, Mark.

In: Cell Cycle, Vol. 10, No. 5, 01.03.2011, p. 783-793.

Research output: Contribution to journalArticle

Mattison, Christopher P. ; Stumpff, Jason ; Wordeman, Linda ; Winey, Mark. / Mip1 associates with both the Mps1 kinase and actin, and is required for cell cortex stability and anaphase spindle positioning. In: Cell Cycle. 2011 ; Vol. 10, No. 5. pp. 783-793.
@article{ca6b7493358a4cebbed3f07fa6a68b6e,
title = "Mip1 associates with both the Mps1 kinase and actin, and is required for cell cortex stability and anaphase spindle positioning",
abstract = "The Mps1 family of protein kinases contributes to cell cycle control by regulating multiple microtubule cytoskeleton activities. We have uncovered a new Mps1 substrate that provides a novel link between Mps1 and the actin cytoskeleton. We have identified a conserved human Mps1 (hMps1) interacting protein and have termed Mps1 interacting protein-1 (Mip1). Mip1 defines an uncharacterized family of conserved proteins that contain coiled-coil and calponin homology domains. We demonstrate that Mip1 is a phosphoprotein that interacts with hMps1 in vitro and in vivo and is a hMps1 substrate. Mip1 exhibits dynamic localization during the cell cycle; Mip1 localizes to the actin cytoskeleton during interphase, the spindle in early mitosis and the cleavage furrow during cytokinesis. Mip1 function is required to ensure proper spindle positioning at the onset of anaphase after cells begin furrow ingression. Cells depleted of Mip1 exhibit aberrant mitotic actin filament organization, excessive membrane blebbing, dramatic spindle rocking and chromosome distribution errors during early cytokinesis producing high numbers of binucleate cells. our data indicate that Mip1 is a newly recognized component of the actin cytoskeleton that interacts with hMps1 and that it is essential to ensure proper segregation of the genome during cell cleavage.",
keywords = "Actin, Cytokinesis, Mip1, Mps1 kinase",
author = "Mattison, {Christopher P.} and Jason Stumpff and Linda Wordeman and Mark Winey",
year = "2011",
month = "3",
day = "1",
doi = "10.4161/cc.10.5.14955",
language = "English (US)",
volume = "10",
pages = "783--793",
journal = "Cell Cycle",
issn = "1538-4101",
publisher = "Landes Bioscience",
number = "5",

}

TY - JOUR

T1 - Mip1 associates with both the Mps1 kinase and actin, and is required for cell cortex stability and anaphase spindle positioning

AU - Mattison, Christopher P.

AU - Stumpff, Jason

AU - Wordeman, Linda

AU - Winey, Mark

PY - 2011/3/1

Y1 - 2011/3/1

N2 - The Mps1 family of protein kinases contributes to cell cycle control by regulating multiple microtubule cytoskeleton activities. We have uncovered a new Mps1 substrate that provides a novel link between Mps1 and the actin cytoskeleton. We have identified a conserved human Mps1 (hMps1) interacting protein and have termed Mps1 interacting protein-1 (Mip1). Mip1 defines an uncharacterized family of conserved proteins that contain coiled-coil and calponin homology domains. We demonstrate that Mip1 is a phosphoprotein that interacts with hMps1 in vitro and in vivo and is a hMps1 substrate. Mip1 exhibits dynamic localization during the cell cycle; Mip1 localizes to the actin cytoskeleton during interphase, the spindle in early mitosis and the cleavage furrow during cytokinesis. Mip1 function is required to ensure proper spindle positioning at the onset of anaphase after cells begin furrow ingression. Cells depleted of Mip1 exhibit aberrant mitotic actin filament organization, excessive membrane blebbing, dramatic spindle rocking and chromosome distribution errors during early cytokinesis producing high numbers of binucleate cells. our data indicate that Mip1 is a newly recognized component of the actin cytoskeleton that interacts with hMps1 and that it is essential to ensure proper segregation of the genome during cell cleavage.

AB - The Mps1 family of protein kinases contributes to cell cycle control by regulating multiple microtubule cytoskeleton activities. We have uncovered a new Mps1 substrate that provides a novel link between Mps1 and the actin cytoskeleton. We have identified a conserved human Mps1 (hMps1) interacting protein and have termed Mps1 interacting protein-1 (Mip1). Mip1 defines an uncharacterized family of conserved proteins that contain coiled-coil and calponin homology domains. We demonstrate that Mip1 is a phosphoprotein that interacts with hMps1 in vitro and in vivo and is a hMps1 substrate. Mip1 exhibits dynamic localization during the cell cycle; Mip1 localizes to the actin cytoskeleton during interphase, the spindle in early mitosis and the cleavage furrow during cytokinesis. Mip1 function is required to ensure proper spindle positioning at the onset of anaphase after cells begin furrow ingression. Cells depleted of Mip1 exhibit aberrant mitotic actin filament organization, excessive membrane blebbing, dramatic spindle rocking and chromosome distribution errors during early cytokinesis producing high numbers of binucleate cells. our data indicate that Mip1 is a newly recognized component of the actin cytoskeleton that interacts with hMps1 and that it is essential to ensure proper segregation of the genome during cell cleavage.

KW - Actin

KW - Cytokinesis

KW - Mip1

KW - Mps1 kinase

UR - http://www.scopus.com/inward/record.url?scp=79952338424&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79952338424&partnerID=8YFLogxK

U2 - 10.4161/cc.10.5.14955

DO - 10.4161/cc.10.5.14955

M3 - Article

VL - 10

SP - 783

EP - 793

JO - Cell Cycle

JF - Cell Cycle

SN - 1538-4101

IS - 5

ER -