Girds 'n' cleeks o' cytokinesis: Microtubule sticks and contractile hoops in cell division

David M. Glover, Luisa Capalbo, Pier Paolo D'Avino, Melanie K. Gatt, Matthew S. Savoian, Tetsuya Takeda

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Microtubules maintain an intimate relationship with the rings of anillin, septins and actomyosin filaments throughout cytokinesis. In Drosophila, peripheral microtubules emanating from the spindle poles contact the equatorial cell cortex to deliver the signal that initiates formation of the cytokinetic furrow. Mutations that affect microtubule stability lead to ectopic furrowing because peripheral microtubules contact inappropriate cortical sites. The PAV-KLP (Pavarotti-kinesin-like protein)/RacGAP50C (where GAP is GTPase-activating protein) centralspindlin complex moves towards the plus ends of microtubules to reach the cell equator. When RacGAP50C is tethered to the cell membrane, furrowing initiates at multiple non-equatorial sites, indicating that mis-localization of this single molecule is sufficient to promote furrowing. Furrow formation and ingression requires RhoA activation by the RhoGEF (guanine-nucleotide-exchange factor) Pebble, which interacts with RacGAP50C. RacGAP50C also binds anillin, which associates with actin, myosin and septins. Thus RacGAP50C plays a pivotal role during furrow formation by activating RhoA and linking the peripheral microtubules with the nascent rings through its interaction with anillin.

Original languageEnglish
Pages (from-to)400-404
Number of pages5
JournalBiochemical Society Transactions
Volume36
Issue number3
DOIs
Publication statusPublished - Jun 2008
Externally publishedYes

Fingerprint

Cytokinesis
Septins
Microtubules
Cell Division
GTPase-Activating Proteins
Cells
Rho Guanine Nucleotide Exchange Factors
Guanine Nucleotide Exchange Factors
Kinesin
Actomyosin
Cell membranes
Myosins
Actins
Poles
Chemical activation
Spindle Poles
Molecules
Drosophila
anillin
Cell Membrane

Keywords

  • Anillin
  • Central-spindle microtubule
  • Centralspindlin
  • Cytokinesis
  • Rac GTPase-activating protein (RacGAP)
  • Rho guanine-nucleotide-exchange factor (RhoGEF)

ASJC Scopus subject areas

  • Biochemistry

Cite this

Girds 'n' cleeks o' cytokinesis : Microtubule sticks and contractile hoops in cell division. / Glover, David M.; Capalbo, Luisa; D'Avino, Pier Paolo; Gatt, Melanie K.; Savoian, Matthew S.; Takeda, Tetsuya.

In: Biochemical Society Transactions, Vol. 36, No. 3, 06.2008, p. 400-404.

Research output: Contribution to journalArticle

Glover, David M. ; Capalbo, Luisa ; D'Avino, Pier Paolo ; Gatt, Melanie K. ; Savoian, Matthew S. ; Takeda, Tetsuya. / Girds 'n' cleeks o' cytokinesis : Microtubule sticks and contractile hoops in cell division. In: Biochemical Society Transactions. 2008 ; Vol. 36, No. 3. pp. 400-404.
@article{c5930e56adbe474a9ef571c774cf0a3a,
title = "Girds 'n' cleeks o' cytokinesis: Microtubule sticks and contractile hoops in cell division",
abstract = "Microtubules maintain an intimate relationship with the rings of anillin, septins and actomyosin filaments throughout cytokinesis. In Drosophila, peripheral microtubules emanating from the spindle poles contact the equatorial cell cortex to deliver the signal that initiates formation of the cytokinetic furrow. Mutations that affect microtubule stability lead to ectopic furrowing because peripheral microtubules contact inappropriate cortical sites. The PAV-KLP (Pavarotti-kinesin-like protein)/RacGAP50C (where GAP is GTPase-activating protein) centralspindlin complex moves towards the plus ends of microtubules to reach the cell equator. When RacGAP50C is tethered to the cell membrane, furrowing initiates at multiple non-equatorial sites, indicating that mis-localization of this single molecule is sufficient to promote furrowing. Furrow formation and ingression requires RhoA activation by the RhoGEF (guanine-nucleotide-exchange factor) Pebble, which interacts with RacGAP50C. RacGAP50C also binds anillin, which associates with actin, myosin and septins. Thus RacGAP50C plays a pivotal role during furrow formation by activating RhoA and linking the peripheral microtubules with the nascent rings through its interaction with anillin.",
keywords = "Anillin, Central-spindle microtubule, Centralspindlin, Cytokinesis, Rac GTPase-activating protein (RacGAP), Rho guanine-nucleotide-exchange factor (RhoGEF)",
author = "Glover, {David M.} and Luisa Capalbo and D'Avino, {Pier Paolo} and Gatt, {Melanie K.} and Savoian, {Matthew S.} and Tetsuya Takeda",
year = "2008",
month = "6",
doi = "10.1042/BST0360400",
language = "English",
volume = "36",
pages = "400--404",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "3",

}

TY - JOUR

T1 - Girds 'n' cleeks o' cytokinesis

T2 - Microtubule sticks and contractile hoops in cell division

AU - Glover, David M.

AU - Capalbo, Luisa

AU - D'Avino, Pier Paolo

AU - Gatt, Melanie K.

AU - Savoian, Matthew S.

AU - Takeda, Tetsuya

PY - 2008/6

Y1 - 2008/6

N2 - Microtubules maintain an intimate relationship with the rings of anillin, septins and actomyosin filaments throughout cytokinesis. In Drosophila, peripheral microtubules emanating from the spindle poles contact the equatorial cell cortex to deliver the signal that initiates formation of the cytokinetic furrow. Mutations that affect microtubule stability lead to ectopic furrowing because peripheral microtubules contact inappropriate cortical sites. The PAV-KLP (Pavarotti-kinesin-like protein)/RacGAP50C (where GAP is GTPase-activating protein) centralspindlin complex moves towards the plus ends of microtubules to reach the cell equator. When RacGAP50C is tethered to the cell membrane, furrowing initiates at multiple non-equatorial sites, indicating that mis-localization of this single molecule is sufficient to promote furrowing. Furrow formation and ingression requires RhoA activation by the RhoGEF (guanine-nucleotide-exchange factor) Pebble, which interacts with RacGAP50C. RacGAP50C also binds anillin, which associates with actin, myosin and septins. Thus RacGAP50C plays a pivotal role during furrow formation by activating RhoA and linking the peripheral microtubules with the nascent rings through its interaction with anillin.

AB - Microtubules maintain an intimate relationship with the rings of anillin, septins and actomyosin filaments throughout cytokinesis. In Drosophila, peripheral microtubules emanating from the spindle poles contact the equatorial cell cortex to deliver the signal that initiates formation of the cytokinetic furrow. Mutations that affect microtubule stability lead to ectopic furrowing because peripheral microtubules contact inappropriate cortical sites. The PAV-KLP (Pavarotti-kinesin-like protein)/RacGAP50C (where GAP is GTPase-activating protein) centralspindlin complex moves towards the plus ends of microtubules to reach the cell equator. When RacGAP50C is tethered to the cell membrane, furrowing initiates at multiple non-equatorial sites, indicating that mis-localization of this single molecule is sufficient to promote furrowing. Furrow formation and ingression requires RhoA activation by the RhoGEF (guanine-nucleotide-exchange factor) Pebble, which interacts with RacGAP50C. RacGAP50C also binds anillin, which associates with actin, myosin and septins. Thus RacGAP50C plays a pivotal role during furrow formation by activating RhoA and linking the peripheral microtubules with the nascent rings through its interaction with anillin.

KW - Anillin

KW - Central-spindle microtubule

KW - Centralspindlin

KW - Cytokinesis

KW - Rac GTPase-activating protein (RacGAP)

KW - Rho guanine-nucleotide-exchange factor (RhoGEF)

UR - http://www.scopus.com/inward/record.url?scp=45249123468&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=45249123468&partnerID=8YFLogxK

U2 - 10.1042/BST0360400

DO - 10.1042/BST0360400

M3 - Article

C2 - 18481968

AN - SCOPUS:45249123468

VL - 36

SP - 400

EP - 404

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 3

ER -