Phosphorylation-dependent regulation of septin dynamics during the cell cycle

Jeroen Dobbelaere; Matthew S. Gentry; Richard L. Hallberg; Yves Barral

doi:10.1016/S1534-5807(03)00061-3

Phosphorylation-dependent regulation of septin dynamics during the cell cycle

Jeroen Dobbelaere
, Matthew S. Gentry
, Richard L. Hallberg
, Yves Barral

Research output: Contribution to journal › Article › peer-review

221 Scopus citations

Abstract

Septins are GTPases involved in cytokinesis. In yeast, they form a ring at the cleavage site. Using FRAP, we show that septins are mobile within the ring at bud emergence and telophase and are immobile during S, G2, and M phases. Immobilization of the septins is dependent on both Cla4, a PAK-like kinase, and Gin4, a septin-dependent kinase that can phosphorylate the septin Shs1/Sep7. Induction of septin ring dynamics in telophase is triggered by the translocation of Rts1, a kinetochore-associated regulatory subunit of PP2A phosphatase, to the bud neck and correlates with Rts1-dependent dephosphorylation of Shs1. In rts1-Δ cells, the actomyosin ring contracts properly but cytokinesis fails. Together our results implicate septins in a late step of cytokinesis and indicate that proper regulation of septin dynamics, possibly through the control of their phosphorylation state, is required for the completion of cytokinesis.

Original language	English
Pages (from-to)	345-357
Number of pages	13
Journal	Developmental Cell
Volume	4
Issue number	3
DOIs	https://doi.org/10.1016/S1534-5807(03)00061-3
State	Published - Mar 1 2003

Bibliographical note

Funding Information:
We thank M. Peter and C. Mann for providing strains, plasmids, and useful suggestions on the manuscript; S. Gasser, S. Jensen, N. Bouquin, D. Kellogg, R. Li, F. Luca, and U. Surana for strains and plasmids; and L. Dowse, S. Grava, R. Kroschewski, U. Kutay, C. Lüdeke, and D. Liakopoulos for critical reading of the manuscript. We thank the members of the Hallberg and Barral groups for helpful discussions. We are particularly indebted to K. Tatchell and E. Bi for communicating unpublished results, S. Cotesta (curve fittings), C. Berney and G. Danuser (FRAP Microscopy), and R. Moser and T. Lehman (technical support). J.D. and Y.B. are supported by the Swiss Federal Institute of Technology and a grant from the Swiss National Foundation. M.S.G. and R.L.H. were supported by National Science Foundation grants MCB-9603733 and MCB-0113355 awarded to R.L.H.

Funding

We thank M. Peter and C. Mann for providing strains, plasmids, and useful suggestions on the manuscript; S. Gasser, S. Jensen, N. Bouquin, D. Kellogg, R. Li, F. Luca, and U. Surana for strains and plasmids; and L. Dowse, S. Grava, R. Kroschewski, U. Kutay, C. L\u00FCdeke, and D. Liakopoulos for critical reading of the manuscript. We thank the members of the Hallberg and Barral groups for helpful discussions. We are particularly indebted to K. Tatchell and E. Bi for communicating unpublished results, S. Cotesta (curve fittings), C. Berney and G. Danuser (FRAP Microscopy), and R. Moser and T. Lehman (technical support). J.D. and Y.B. are supported by the Swiss Federal Institute of Technology and a grant from the Swiss National Foundation. M.S.G. and R.L.H. were supported by National Science Foundation grants MCB-9603733 and MCB-0113355 awarded to R.L.H.

Funders	Funder number
Swiss Federal Institute of Technology
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
U.S. Department of Energy Chinese Academy of Sciences Guangzhou Municipal Science and Technology Project Oak Ridge National Laboratory Extreme Science and Engineering Discovery Environment National Science Foundation National Energy Research Scientific Computing Center National Natural Science Foundation of China	MCB-0113355, MCB-9603733

ASJC Scopus subject areas

Molecular Biology
General Biochemistry, Genetics and Molecular Biology
Developmental Biology
Cell Biology

Access to Document

10.1016/S1534-5807(03)00061-3

Cite this

@article{ed05ef07add04f6496b42e717d9b23bf,

title = "Phosphorylation-dependent regulation of septin dynamics during the cell cycle",

abstract = "Septins are GTPases involved in cytokinesis. In yeast, they form a ring at the cleavage site. Using FRAP, we show that septins are mobile within the ring at bud emergence and telophase and are immobile during S, G2, and M phases. Immobilization of the septins is dependent on both Cla4, a PAK-like kinase, and Gin4, a septin-dependent kinase that can phosphorylate the septin Shs1/Sep7. Induction of septin ring dynamics in telophase is triggered by the translocation of Rts1, a kinetochore-associated regulatory subunit of PP2A phosphatase, to the bud neck and correlates with Rts1-dependent dephosphorylation of Shs1. In rts1-Δ cells, the actomyosin ring contracts properly but cytokinesis fails. Together our results implicate septins in a late step of cytokinesis and indicate that proper regulation of septin dynamics, possibly through the control of their phosphorylation state, is required for the completion of cytokinesis.",

author = "Jeroen Dobbelaere and Gentry, \{Matthew S.\} and Hallberg, \{Richard L.\} and Yves Barral",

note = "Funding Information: We thank M. Peter and C. Mann for providing strains, plasmids, and useful suggestions on the manuscript; S. Gasser, S. Jensen, N. Bouquin, D. Kellogg, R. Li, F. Luca, and U. Surana for strains and plasmids; and L. Dowse, S. Grava, R. Kroschewski, U. Kutay, C. L{\"u}deke, and D. Liakopoulos for critical reading of the manuscript. We thank the members of the Hallberg and Barral groups for helpful discussions. We are particularly indebted to K. Tatchell and E. Bi for communicating unpublished results, S. Cotesta (curve fittings), C. Berney and G. Danuser (FRAP Microscopy), and R. Moser and T. Lehman (technical support). J.D. and Y.B. are supported by the Swiss Federal Institute of Technology and a grant from the Swiss National Foundation. M.S.G. and R.L.H. were supported by National Science Foundation grants MCB-9603733 and MCB-0113355 awarded to R.L.H.",

year = "2003",

month = mar,

day = "1",

doi = "10.1016/S1534-5807(03)00061-3",

language = "English",

volume = "4",

pages = "345--357",

number = "3",

}

TY - JOUR

T1 - Phosphorylation-dependent regulation of septin dynamics during the cell cycle

AU - Dobbelaere, Jeroen

AU - Gentry, Matthew S.

AU - Hallberg, Richard L.

AU - Barral, Yves

N1 - Funding Information: We thank M. Peter and C. Mann for providing strains, plasmids, and useful suggestions on the manuscript; S. Gasser, S. Jensen, N. Bouquin, D. Kellogg, R. Li, F. Luca, and U. Surana for strains and plasmids; and L. Dowse, S. Grava, R. Kroschewski, U. Kutay, C. Lüdeke, and D. Liakopoulos for critical reading of the manuscript. We thank the members of the Hallberg and Barral groups for helpful discussions. We are particularly indebted to K. Tatchell and E. Bi for communicating unpublished results, S. Cotesta (curve fittings), C. Berney and G. Danuser (FRAP Microscopy), and R. Moser and T. Lehman (technical support). J.D. and Y.B. are supported by the Swiss Federal Institute of Technology and a grant from the Swiss National Foundation. M.S.G. and R.L.H. were supported by National Science Foundation grants MCB-9603733 and MCB-0113355 awarded to R.L.H.

PY - 2003/3/1

Y1 - 2003/3/1

N2 - Septins are GTPases involved in cytokinesis. In yeast, they form a ring at the cleavage site. Using FRAP, we show that septins are mobile within the ring at bud emergence and telophase and are immobile during S, G2, and M phases. Immobilization of the septins is dependent on both Cla4, a PAK-like kinase, and Gin4, a septin-dependent kinase that can phosphorylate the septin Shs1/Sep7. Induction of septin ring dynamics in telophase is triggered by the translocation of Rts1, a kinetochore-associated regulatory subunit of PP2A phosphatase, to the bud neck and correlates with Rts1-dependent dephosphorylation of Shs1. In rts1-Δ cells, the actomyosin ring contracts properly but cytokinesis fails. Together our results implicate septins in a late step of cytokinesis and indicate that proper regulation of septin dynamics, possibly through the control of their phosphorylation state, is required for the completion of cytokinesis.

AB - Septins are GTPases involved in cytokinesis. In yeast, they form a ring at the cleavage site. Using FRAP, we show that septins are mobile within the ring at bud emergence and telophase and are immobile during S, G2, and M phases. Immobilization of the septins is dependent on both Cla4, a PAK-like kinase, and Gin4, a septin-dependent kinase that can phosphorylate the septin Shs1/Sep7. Induction of septin ring dynamics in telophase is triggered by the translocation of Rts1, a kinetochore-associated regulatory subunit of PP2A phosphatase, to the bud neck and correlates with Rts1-dependent dephosphorylation of Shs1. In rts1-Δ cells, the actomyosin ring contracts properly but cytokinesis fails. Together our results implicate septins in a late step of cytokinesis and indicate that proper regulation of septin dynamics, possibly through the control of their phosphorylation state, is required for the completion of cytokinesis.

UR - https://www.scopus.com/pages/publications/0037345639

UR - https://www.scopus.com/pages/publications/0037345639#tab=citedBy

U2 - 10.1016/S1534-5807(03)00061-3

DO - 10.1016/S1534-5807(03)00061-3

M3 - Article

C2 - 12636916

AN - SCOPUS:0037345639

SN - 1534-5807

VL - 4

SP - 345

EP - 357

JO - Developmental Cell

JF - Developmental Cell

IS - 3

ER -

Phosphorylation-dependent regulation of septin dynamics during the cell cycle

Abstract

Bibliographical note

Funding

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this