Sid4p-Cdc11p assembles the septation initiation network and its regulators at the S. pombe SPB

Jennifer L. Morrell; Gregory C. Tomlin; Srividya Rajagopalan; Srinivas Venkatram; Anna S. Feoktistova; Joseph J. Tasto; Sapna Mehta; Jennifer L. Jennings; Andrew Link; Mohan K. Balasubramanian; Kathleen L. Gould

doi:10.1016/j.cub.2004.03.036

Sid4p-Cdc11p assembles the septation initiation network and its regulators at the S. pombe SPB

Jennifer L. Morrell, Gregory C. Tomlin, Srividya Rajagopalan, Srinivas Venkatram, Anna S. Feoktistova, Joseph J. Tasto, Sapna Mehta, Jennifer L. Jennings, Andrew Link, Mohan K. Balasubramanian, Kathleen L. Gould

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

64 Scopus citations

Abstract

The Schizosaccharomyces pombe septation initiation network (SIN) triggers actomyosin ring constriction, septation, and cell division. It is organized at the spindle pole body (SPB) by the scaffold proteins Sid4p and Cdc11p. Here, we dissect the contributions of Sid4p and Cdc11p in anchoring SIN components and SIN regulators to the SPB. We find that Sid4p interacts with the SIN activator, Plo1p, in addition to Cdc11p and Dma1p. While the C terminus of Cdc11p is involved in binding Sid4p, its N-terminal half is involved in a wide variety of direct protein-protein interactions, including those with Spg1p, Sid2p, Cdc16p, and Cdk1p-Cdc13p. Given that the localizations of the remaining SIN components depend on Spg1p or Cdc16p, these data allow us to build a comprehensive model of SIN component organization at the SPB. FRAP experiments indicate that Sid4p and Cdc11p are stable SPB components, whereas signaling components of the SIN are dynamically associated with these structures. Our results suggest that the Sid4p-Cdc11p complex organizes a signaling hub on the SPB and that this hub coordinates cell and nuclear division.

Original language	English
Pages (from-to)	579-584
Number of pages	6
Journal	Current Biology
Volume	14
Issue number	7
DOIs	https://doi.org/10.1016/j.cub.2004.03.036
State	Published - Apr 6 2004
Externally published	Yes

Funding

The authors are grateful to Dan McCollum for sharing unpublished results, members of the Gould lab for critical comments on the manuscript and helpful discussions, and J. Liu for help with image analysis. J.L.J. is supported by National Institutes of Health grants GM64779 and HL68744. A.J.L. is supported by National Institutes of Health grants GM64779, HL68744, NS43952, ES11993, and CA098131. M.K.B. was supported by research funds from the Temasek Life Science Laboratory. Work in the Gould lab was supported by the Howard Hughes Medical Institute, of which K.L.G. is an Investigator.

Funders	Funder number
National Institutes of Health	GM64779, HL68744, CA098131, NS43952
Howard Hughes Medical Institute
National Institute of Environmental Health Sciences	R01ES011993
Temasek Life Sciences Laboratory

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title = "Sid4p-Cdc11p assembles the septation initiation network and its regulators at the S. pombe SPB",

abstract = "The Schizosaccharomyces pombe septation initiation network (SIN) triggers actomyosin ring constriction, septation, and cell division. It is organized at the spindle pole body (SPB) by the scaffold proteins Sid4p and Cdc11p. Here, we dissect the contributions of Sid4p and Cdc11p in anchoring SIN components and SIN regulators to the SPB. We find that Sid4p interacts with the SIN activator, Plo1p, in addition to Cdc11p and Dma1p. While the C terminus of Cdc11p is involved in binding Sid4p, its N-terminal half is involved in a wide variety of direct protein-protein interactions, including those with Spg1p, Sid2p, Cdc16p, and Cdk1p-Cdc13p. Given that the localizations of the remaining SIN components depend on Spg1p or Cdc16p, these data allow us to build a comprehensive model of SIN component organization at the SPB. FRAP experiments indicate that Sid4p and Cdc11p are stable SPB components, whereas signaling components of the SIN are dynamically associated with these structures. Our results suggest that the Sid4p-Cdc11p complex organizes a signaling hub on the SPB and that this hub coordinates cell and nuclear division.",

author = "Morrell, {Jennifer L.} and Tomlin, {Gregory C.} and Srividya Rajagopalan and Srinivas Venkatram and Feoktistova, {Anna S.} and Tasto, {Joseph J.} and Sapna Mehta and Jennings, {Jennifer L.} and Andrew Link and Balasubramanian, {Mohan K.} and Gould, {Kathleen L.}",

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AU - Morrell, Jennifer L.

AU - Tomlin, Gregory C.

AU - Rajagopalan, Srividya

AU - Venkatram, Srinivas

AU - Feoktistova, Anna S.

AU - Tasto, Joseph J.

AU - Mehta, Sapna

AU - Jennings, Jennifer L.

AU - Link, Andrew

AU - Balasubramanian, Mohan K.

AU - Gould, Kathleen L.

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N2 - The Schizosaccharomyces pombe septation initiation network (SIN) triggers actomyosin ring constriction, septation, and cell division. It is organized at the spindle pole body (SPB) by the scaffold proteins Sid4p and Cdc11p. Here, we dissect the contributions of Sid4p and Cdc11p in anchoring SIN components and SIN regulators to the SPB. We find that Sid4p interacts with the SIN activator, Plo1p, in addition to Cdc11p and Dma1p. While the C terminus of Cdc11p is involved in binding Sid4p, its N-terminal half is involved in a wide variety of direct protein-protein interactions, including those with Spg1p, Sid2p, Cdc16p, and Cdk1p-Cdc13p. Given that the localizations of the remaining SIN components depend on Spg1p or Cdc16p, these data allow us to build a comprehensive model of SIN component organization at the SPB. FRAP experiments indicate that Sid4p and Cdc11p are stable SPB components, whereas signaling components of the SIN are dynamically associated with these structures. Our results suggest that the Sid4p-Cdc11p complex organizes a signaling hub on the SPB and that this hub coordinates cell and nuclear division.

AB - The Schizosaccharomyces pombe septation initiation network (SIN) triggers actomyosin ring constriction, septation, and cell division. It is organized at the spindle pole body (SPB) by the scaffold proteins Sid4p and Cdc11p. Here, we dissect the contributions of Sid4p and Cdc11p in anchoring SIN components and SIN regulators to the SPB. We find that Sid4p interacts with the SIN activator, Plo1p, in addition to Cdc11p and Dma1p. While the C terminus of Cdc11p is involved in binding Sid4p, its N-terminal half is involved in a wide variety of direct protein-protein interactions, including those with Spg1p, Sid2p, Cdc16p, and Cdk1p-Cdc13p. Given that the localizations of the remaining SIN components depend on Spg1p or Cdc16p, these data allow us to build a comprehensive model of SIN component organization at the SPB. FRAP experiments indicate that Sid4p and Cdc11p are stable SPB components, whereas signaling components of the SIN are dynamically associated with these structures. Our results suggest that the Sid4p-Cdc11p complex organizes a signaling hub on the SPB and that this hub coordinates cell and nuclear division.

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Sid4p-Cdc11p assembles the septation initiation network and its regulators at the S. pombe SPB

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