Difference between revisions of "YMR109W"

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'''Description of YMR109W:''' One of two type I myosins; contains proline-rich tail homology 2 (TH2) and SH3 domains; MYO5 deletion has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization<ref name='S000073475'>Tanaka K and Matsui Y (2001) Functions of unconventional myosins in the yeast Saccharomyces cerevisiae. Cell Struct Funct 26(6):671-5 {{SGDpaper|S000073475}} PMID 11942625</ref><ref name='S000040780'>Anderson BL, et al. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol 141(6):1357-70 {{SGDpaper|S000040780}} PMID 9628892</ref><ref name='S000039647'>Geli MI and Riezman H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272(5261):533-5
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'''Description of YMR109W:''' One of two type I myosins; contains proline-rich tail homology 2 (TH2) and SH3 domains; MYO5 deletion has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization<ref name='S000039647'>Geli MI and Riezman H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272(5261):533-5 {{SGDpaper|S000039647}} PMID 8614799</ref><ref name='S000040780'>Anderson BL, et al. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol 141(6):1357-70 {{SGDpaper|S000040780}} PMID 9628892</ref><ref name='S000073475'>Tanaka K and Matsui Y (2001) Functions of unconventional myosins in the yeast Saccharomyces cerevisiae. Cell Struct Funct 26(6):671-5
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  {{SGDpaper|S000073475}} PMID 11942625</ref>
 
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Revision as of 13:05, 31 March 2009

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Systematic name YMR109W
Gene name MYO5
Aliases
Feature type ORF, Verified
Coordinates Chr XIII:486586..490245
Primary SGDID S000004715


Description of YMR109W: One of two type I myosins; contains proline-rich tail homology 2 (TH2) and SH3 domains; MYO5 deletion has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization[1][2][3]




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References

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  1. Geli MI and Riezman H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272(5261):533-5 SGD PMID 8614799
  2. Anderson BL, et al. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol 141(6):1357-70 SGD PMID 9628892
  3. Tanaka K and Matsui Y (2001) Functions of unconventional myosins in the yeast Saccharomyces cerevisiae. Cell Struct Funct 26(6):671-5 SGD PMID 11942625

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