Abstract
Schizosaccharomyces pombe defective in phosphatidylinositol (PtdIns) 3-kinase shows various defects in forespore membrane formation, including onset, growth orientation, and closure. Downstream factors of PtdIns 3-kinase in this system were explored. Among various phox homology (PX) domain-containing proteins, Vps5p and Vps17p, homologues of sorting nexins, were found to be required for efficient sporulation. Cells defective in these proteins showed a disordered growth orientation of the forespore membrane, as is the case with Δpik3 cells. Vps5p and Vps17p with mutations in the PX domains failed to suppress the defects of their relevant disruptants. Vps5p and Vps17p migrated toward the the forespore membrane in a pik3+-dependent manner, suggesting that these proteins may interact with PtdIns(3)P. Electron-microscopic analysis revealed that the forespore membrane fails to engulf the nucleus in some of these cells, accumulating vesicle-like bodies similar to those seen in Δspo3 cells. These results suggest that Vps5p and Vps17p are the targets of PtdIns(3)P in vesicle transport required for onset of the forespore membrane formation.
| Original language | English |
|---|---|
| Pages (from-to) | 561-574 |
| Number of pages | 14 |
| Journal | Genes to Cells |
| Volume | 9 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Jun 1 2004 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Genetics
- Cell Biology
Cite this
Sorting nexin homologues are targets of phosphatidylinositol 3-phosphate in sporulation of Schizosaccharomyces pombe. / Koga, Takako; Onishi, Masayuki; Nakamura, Yoko; Hirata, Aiko; Nakamura, Taro; Shimoda, Chikashi; Iwaki, Tomoko; Takegawa, Kaoru; Fukui, Yasushisa.
In: Genes to Cells, Vol. 9, No. 6, 01.06.2004, p. 561-574.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Sorting nexin homologues are targets of phosphatidylinositol 3-phosphate in sporulation of Schizosaccharomyces pombe
AU - Koga, Takako
AU - Onishi, Masayuki
AU - Nakamura, Yoko
AU - Hirata, Aiko
AU - Nakamura, Taro
AU - Shimoda, Chikashi
AU - Iwaki, Tomoko
AU - Takegawa, Kaoru
AU - Fukui, Yasushisa
PY - 2004/6/1
Y1 - 2004/6/1
N2 - Schizosaccharomyces pombe defective in phosphatidylinositol (PtdIns) 3-kinase shows various defects in forespore membrane formation, including onset, growth orientation, and closure. Downstream factors of PtdIns 3-kinase in this system were explored. Among various phox homology (PX) domain-containing proteins, Vps5p and Vps17p, homologues of sorting nexins, were found to be required for efficient sporulation. Cells defective in these proteins showed a disordered growth orientation of the forespore membrane, as is the case with Δpik3 cells. Vps5p and Vps17p with mutations in the PX domains failed to suppress the defects of their relevant disruptants. Vps5p and Vps17p migrated toward the the forespore membrane in a pik3+-dependent manner, suggesting that these proteins may interact with PtdIns(3)P. Electron-microscopic analysis revealed that the forespore membrane fails to engulf the nucleus in some of these cells, accumulating vesicle-like bodies similar to those seen in Δspo3 cells. These results suggest that Vps5p and Vps17p are the targets of PtdIns(3)P in vesicle transport required for onset of the forespore membrane formation.
AB - Schizosaccharomyces pombe defective in phosphatidylinositol (PtdIns) 3-kinase shows various defects in forespore membrane formation, including onset, growth orientation, and closure. Downstream factors of PtdIns 3-kinase in this system were explored. Among various phox homology (PX) domain-containing proteins, Vps5p and Vps17p, homologues of sorting nexins, were found to be required for efficient sporulation. Cells defective in these proteins showed a disordered growth orientation of the forespore membrane, as is the case with Δpik3 cells. Vps5p and Vps17p with mutations in the PX domains failed to suppress the defects of their relevant disruptants. Vps5p and Vps17p migrated toward the the forespore membrane in a pik3+-dependent manner, suggesting that these proteins may interact with PtdIns(3)P. Electron-microscopic analysis revealed that the forespore membrane fails to engulf the nucleus in some of these cells, accumulating vesicle-like bodies similar to those seen in Δspo3 cells. These results suggest that Vps5p and Vps17p are the targets of PtdIns(3)P in vesicle transport required for onset of the forespore membrane formation.
UR - http://www.scopus.com/inward/record.url?scp=3042858919&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=3042858919&partnerID=8YFLogxK
U2 - 10.1111/j.1356-9597.2004.00744.x
DO - 10.1111/j.1356-9597.2004.00744.x
M3 - Article
C2 - 15189449
AN - SCOPUS:3042858919
VL - 9
SP - 561
EP - 574
JO - Genes to Cells
JF - Genes to Cells
SN - 1356-9597
IS - 6
ER -