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  • CDC24 gene  (1)
  • Cell Membrane/metabolism  (1)
  • 1995-1999  (2)
  • 1
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    Molecular identification of a eukaryotic, stretch-activated nonselective cation channel (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-07
    Description: Calcium-permeable, stretch-activated nonselective cation (SA Cat) channels mediate cellular responses to mechanical stimuli. However, genes encoding such channels have not been identified in eukaryotes. The yeast MID1 gene product (Mid1) is required for calcium influx in the yeast Saccharomyces cerevisiae. Functional expression of Mid1 in Chinese hamster ovary cells conferred sensitivity to mechanical stress that resulted in increases in both calcium conductance and the concentration of cytosolic free calcium. These increases were dependent on the presence of extracellular calcium and were reduced by gadolinium, a blocker of SA Cat channels. Single-channel analyses with cell-attached patches revealed that Mid1 acts as a calcium-permeable, cation-selective stretch-activated channel with a conductance of 32 picosiemens at 150 millimolar cesium chloride in the pipette. Thus, Mid1 appears to be a eukaryotic, SA Cat channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanzaki, M -- Nagasawa, M -- Kojima, I -- Sato, C -- Naruse, K -- Sokabe, M -- Iida, H -- New York, N.Y. -- Science. 1999 Aug 6;285(5429):882-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma 371-8510, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10436155" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Calcium/metabolism ; Calcium Channels/chemistry/genetics/*metabolism ; Cations/*metabolism ; Cell Membrane/metabolism ; Cell Membrane Permeability ; Cesium/metabolism ; Chlorides/pharmacology ; Cricetinae ; Fungal Proteins/chemistry/genetics/*metabolism ; Gadolinium/pharmacology ; Ion Channels/chemistry/genetics/*metabolism ; Membrane Glycoproteins/chemistry/genetics/*metabolism ; Membrane Potentials ; Molecular Sequence Data ; Patch-Clamp Techniques ; Pressure ; Saccharomyces cerevisiae/genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Stress, Mechanical ; Transfection ; Zinc Compounds/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
    Electronic Resource
    Electronic Resource
    Overproduction of Cdc24p (Cls4p), a guanine nucleotide-exchange factor toward Cdc42 GTPase, impairs initiation of budding inSaccharomyces cerevisiae (1995)
    Springer
    Protoplasma 189 (1995), S. 142-148 
    Details
    ISSN: 1615-6102
    Keywords: Cell polarity ; Budding yeast ; Calcium ; CLS4 gene ; CDC24 gene ; Overexpression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary An entire coding region of theCDC24/CLS4 gene and its truncated derivatives were overexpressed in yeast cells under the control of theGAL1 promoter. Western blotting analysis of the yeast cell lysates showed that the CDC24/CLS4 protein (Cdc24p) was induced to reach its maximum level after 9 h incubation of the cells in galactose medium. Overexpression of Cdc24p within the cells caused the morphological change, accumulating large spherical unbudded cells which exhibited actin cytoskeleton disturbed, chitin delocalized on the cell surface, and cell viability decreased. Multiple nuclei were observed in these cells, indicating that only budding cycle but not nuclear division cycle is blocked by the overproduction of Cdc24p. In order to identify the region of Cdc24p responsible for the growth inhibition, several truncatedCDC24 genes were expressed. Surprisingly, overexpression of fragments either containing the C-terminal 76 amino acid residues or deleting the same region inhibited cellular growth. This suggests that Cdc24p contains multiple functional domains for its tasks, likely cooperating signals of bud positioning and bud timing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01280167
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