Contractile Ring Stability in S. pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex
Cdc15p is known to contribute to cytokinesis in fission yeast; however, the protein is not required to assemble the contractile ring of actin and myosin, but it helps to anchor the ring to the plasma membrane. Cdc15p has a lipid-binding F-BAR domain, suggesting that it provides a physical link betwe...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2014-09-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124714006329 |
| _version_ | 1830300652501204992 |
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| author | Rajesh Arasada Thomas D. Pollard |
| author_facet | Rajesh Arasada Thomas D. Pollard |
| author_sort | Rajesh Arasada |
| collection | DOAJ |
| description | Cdc15p is known to contribute to cytokinesis in fission yeast; however, the protein is not required to assemble the contractile ring of actin and myosin, but it helps to anchor the ring to the plasma membrane. Cdc15p has a lipid-binding F-BAR domain, suggesting that it provides a physical link between the plasma membrane and contractile ring proteins. However, we find that a more important function of Cdc15p during cytokinesis is to help deliver a transmembrane enzyme, Bgs1p (also called Cps1p), from the Golgi apparatus to the plasma membrane, where it appears to anchor the contractile ring. Bgs1p synthesizes the cell wall in the cleavage furrow, but its enzyme activity is not required to anchor the contractile ring. We estimate that ∼2,000 Bgs1p molecules are required to anchor the ring. Without Bgs1p anchors, contractile rings slide along the plasma membrane, a phenomenon that depends on an unconventional type II myosin called Myp2p. |
| first_indexed | 2024-12-19T08:32:55Z |
| format | Article |
| id | doaj.art-a467ad29757641399befb5e3749f9e6b |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-19T08:32:55Z |
| publishDate | 2014-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-a467ad29757641399befb5e3749f9e6b2022-12-21T20:29:08ZengElsevierCell Reports2211-12472014-09-01851533154410.1016/j.celrep.2014.07.048Contractile Ring Stability in S. pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi ComplexRajesh Arasada0Thomas D. Pollard1Department of Molecular Cellular and Developmental Biology, Yale University, P.O. Box 208103, New Haven, CT 06520-8103 USADepartment of Molecular Cellular and Developmental Biology, Yale University, P.O. Box 208103, New Haven, CT 06520-8103 USACdc15p is known to contribute to cytokinesis in fission yeast; however, the protein is not required to assemble the contractile ring of actin and myosin, but it helps to anchor the ring to the plasma membrane. Cdc15p has a lipid-binding F-BAR domain, suggesting that it provides a physical link between the plasma membrane and contractile ring proteins. However, we find that a more important function of Cdc15p during cytokinesis is to help deliver a transmembrane enzyme, Bgs1p (also called Cps1p), from the Golgi apparatus to the plasma membrane, where it appears to anchor the contractile ring. Bgs1p synthesizes the cell wall in the cleavage furrow, but its enzyme activity is not required to anchor the contractile ring. We estimate that ∼2,000 Bgs1p molecules are required to anchor the ring. Without Bgs1p anchors, contractile rings slide along the plasma membrane, a phenomenon that depends on an unconventional type II myosin called Myp2p.http://www.sciencedirect.com/science/article/pii/S2211124714006329 |
| spellingShingle | Rajesh Arasada Thomas D. Pollard Contractile Ring Stability in S. pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex Cell Reports |
| title | Contractile Ring Stability in S. pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex |
| title_full | Contractile Ring Stability in S. pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex |
| title_fullStr | Contractile Ring Stability in S. pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex |
| title_full_unstemmed | Contractile Ring Stability in S. pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex |
| title_short | Contractile Ring Stability in S. pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex |
| title_sort | contractile ring stability in s pombe depends on f bar protein cdc15p and bgs1p transport from the golgi complex |
| url | http://www.sciencedirect.com/science/article/pii/S2211124714006329 |
| work_keys_str_mv | AT rajesharasada contractileringstabilityinspombedependsonfbarproteincdc15pandbgs1ptransportfromthegolgicomplex AT thomasdpollard contractileringstabilityinspombedependsonfbarproteincdc15pandbgs1ptransportfromthegolgicomplex |