Research Project
Grant-in-Aid for Scientific Research (B)
1) The amino acid residue Phe^<356> of the putative stretch-activated Ca^<2+> channel Mid1 was determined to be important for cell viability in yeast. Systematic substitution of various amino acids for Phe^<355> revealed that hydrophobicity of this residue is critical.2) The Mid1 protein was found to be localized to the plasma membrane and endoplasmic reticulum membrane. Mid1 forms a oligomer via disulfide bonding.3) A multicopy suppressor of the mid1 mutation was isolated and characterized. This multicopy suppressor is an N-terminally truncated form of the Spa2 protein important for polarized morphgenesis.4) A gene encoding Cch1, which has been genetically suggested to function with Mid1 as a Ca^<2+> channel, was cloned. We have confirmed that Mid1 and Cch1 really cooperate to function as a Ca^<2+> channel.5) Rice OsTpc1 that is homologous to yeast Cch1 was found to be sensitive to blockers of L-type voltage-gated calcium channels. In addition, The Arabidopsis Mca1 protein, which can complement the lethality of the yeast mid1 mutant, was isolated and characterized. Mca1 is crucial for Ca^<2+> influx and touch sensing in primary roots.
All 2007 2005 2004
All Journal Article (27 results) Book (3 results)
Proc. Natl. Acad. Sci. USA 104
Pages: 3639-3644
Proc.Natl.Acad.Sci.USA 104
Eukaryot. Cell 4
Pages: 1353-1363
Plant Biotechnol. 22
Pages: 235-239
10028053758
Exp. Cell Res. 311
Pages: 84-95
Exp.Cell Res. 311
Eukaryot.Cell 4
Eukaryotic Cell 4
Plant Biotechnology 22
Experimental Cell Research 311
Biochem. Biophs. Res. Commun 313
Pages: 752-757
Exp. Cell Res. 293
Pages: 185-195
Plant Cell Physiol. 45
Pages: 496-500
10012852684
Pages: 1704-1708
10014020982
FEBS Lett. 576
Pages: 291-296
Exp.Cell Res. 293
Biochem.Biophys.Res.Commun. 313
J.Biol.Chem. 313
Exp.Cell Res 293