Please use this identifier to cite or link to this item:
Title: A New Membrane Protein Sbg1 Links the Contractile Ring Apparatus and Septum Synthesis Machinery in Fission Yeast
Authors: Sethi K. 
Palani S.
Cortés J.C.G.
Sato M.
Sevugan M.
Ramos M.
Vijaykumar S.
Osumi M.
Naqvi N.I. 
Ribas J.C.
Balasubramanian M.
Keywords: 1,3 beta glucan synthase
membrane protein
protein Bgs1p
protein Cdc15p
protein Cps1p
protein Imp2p
protein Pxl1p
protein Rga7p
suppressor of beta glucan synthase 1
suppressor of beta glucan synthase 1p
unclassified drug
1,3-beta-glucan synthase
beta glucan
cell cycle protein
membrane protein
myosin adenosine triphosphatase
Sbg1 protein, S pombe
Schizosaccharomyces pombe protein
cell membrane
colony formation
contractile ring apparatus
controlled study
essential gene
fungal cell wall
fungal structures
high temperature
protein depletion
protein localization
protein protein interaction
Schizosaccharomyces pombe
septum synthesis
actin filament
cell division
cell wall
Actin Cytoskeleton
Cell Cycle Proteins
Cell Division
Cell Membrane
Cell Wall
Membrane Proteins
Schizosaccharomyces pombe Proteins
Issue Date: 2016
Publisher: Public Library of Science
Citation: Sethi K., Palani S., Cortés J.C.G., Sato M., Sevugan M., Ramos M., Vijaykumar S., Osumi M., Naqvi N.I., Ribas J.C., Balasubramanian M. (2016). A New Membrane Protein Sbg1 Links the Contractile Ring Apparatus and Septum Synthesis Machinery in Fission Yeast. PLoS Genetics 12 (10) : e1006383. ScholarBank@NUS Repository.
Abstract: Cytokinesis in many organisms requires a plasma membrane anchored actomyosin ring, whose contraction facilitates cell division. In yeast and fungi, actomyosin ring constriction is also coordinated with division septum assembly. How the actomyosin ring interacts with the plasma membrane and the plasma membrane-localized septum synthesizing machinery remains poorly understood. In Schizosaccharomyces pombe, an attractive model organism to study cytokinesis, the β-1,3-glucan synthase Cps1p / Bgs1p, an integral membrane protein, localizes to the plasma membrane overlying the actomyosin ring and is required for primary septum synthesis. Through a high-dosage suppressor screen we identified an essential gene, sbg1+ (suppressor of beta glucan synthase 1), which suppressed the colony formation defect of Bgs1-defective cps1-191 mutant at higher temperatures. Sbg1p, an integral membrane protein, localizes to the cell ends and to the division site. Sbg1p and Bgs1p physically interact and are dependent on each other to localize to the division site. Loss of Sbg1p results in an unstable actomyosin ring that unravels and slides, leading to an inability to deposit a single contiguous division septum and an important reduction of the β-1,3-glucan proportion in the cell wall, coincident with that observed in the cps1-191 mutant. Sbg1p shows genetic and / or physical interaction with Rga7p, Imp2p, Cdc15p, and Pxl1p, proteins known to be required for actomyosin ring integrity and efficient septum synthesis. This study establishes Sbg1p as a key member of a group of proteins that link the plasma membrane, the actomyosin ring, and the division septum assembly machinery in fission yeast. © 2016 Sethi et al.
Source Title: PLoS Genetics
ISSN: 15537390
DOI: 10.1371/journal.pgen.1006383
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1371_journal_pgen_1006383.pdf4.03 MBAdobe PDF




checked on Oct 23, 2020

Page view(s)

checked on Oct 16, 2020

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.