| Project/Area Number |
16590236
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | Shujitsu University |
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Principal Investigator |
KOYAMA Shinya Shujitsu University, Faculty of Pharmacology, Professor, 薬学部, 教授 (00186834)
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| Project Period (FY) |
2004 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2005: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2004: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | Ent1 / Eps15 / POB1 / vesicule translocation |
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| Research Abstract |
POB1(Reps2) is supposed to function downstream of Ras in regulation of receptor-endocytosis and intracellular vesicle translocation. To clear the mechanism of the function, POB1-binding proteins were screened from mammalian cDNA libraries by yeast two-hybrid method, and several SH3 proteins were selected as candidates : Endophilin(SH3GL2, an Eps15-binding protein), Snapin (a SNAP25-binding protein), Ese2(Intersectin), SH3yl1. Then dissociation constants to POB 1 of these proteins are measured in HEPS-buffered saline (pH7.4) at 25℃.
The results were :
RaIBP1(positive control):0.8 nM ;
Endophilin:0.46 uM ; Snapin:9.7 uM ; Ese2:0.98 uM ;
SH3yl1:3.04 nM
These results suggests that SH3GL2, Snapin and Ese2 hardly react directly with POB1, and that SH3yl1 reacts directly with POB1 under the physiolosical condition.
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