Source:http://linkedlifedata.com/resource/pubmed/id/17458633
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3-4
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pubmed:dateCreated |
2007-4-26
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pubmed:abstractText |
Phenylarsine oxide (PAO) and genistein are two well-known specific inhibitors of tyrosine phosphatases and kinases, respectively, that have been used in the functional analysis of the status of protein phosphotyrosine in different cell types. Our experiments showed that both PAO and genistein arrested pollen germination and pollen tube growth and led to the malformation of the pollen tubes, although genistein had a lesser effect. The malformations of the pollen tubes caused by PAO and genistein were, however, quite different. In addition, it was found that the rate of pollen germination and tube growth recovered to a certain extent when phalloidin was present during PAO treatment, but not when it was present during genistein treatment. Furthermore, PAO treatment also had a great effect on the dynamic organization of filamentous actin in the pollen grain and pollen tube, while genistein only caused reorganization of actin at the turning point of the pollen tube. Our results suggest that reversible protein tyrosine phosphorylation is a crucial step in pollen germination and pollen tube growth, but that tyrosine kinases and phosphatases may have different effects which may function through the reorganization of the actin cytoskeleton.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Arsenicals,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Genistein,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/oxophenylarsine
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pubmed:status |
MEDLINE
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pubmed:issn |
0033-183X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
230
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
183-91
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:17458633-Actins,
pubmed-meshheading:17458633-Arsenicals,
pubmed-meshheading:17458633-Cell Differentiation,
pubmed-meshheading:17458633-Cell Polarity,
pubmed-meshheading:17458633-Cytoskeleton,
pubmed-meshheading:17458633-Enzyme Inhibitors,
pubmed-meshheading:17458633-Genistein,
pubmed-meshheading:17458633-Germination,
pubmed-meshheading:17458633-Lilium,
pubmed-meshheading:17458633-Phosphorylation,
pubmed-meshheading:17458633-Pollen,
pubmed-meshheading:17458633-Pollen Tube,
pubmed-meshheading:17458633-Protein Tyrosine Phosphatases,
pubmed-meshheading:17458633-Protoplasts,
pubmed-meshheading:17458633-Tyrosine
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pubmed:year |
2007
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pubmed:articleTitle |
Reversible protein tyrosine phosphorylation affects pollen germination and pollen tube growth via the actin cytoskeleton.
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pubmed:affiliation |
Key Laboratory of Cell Proliferation and Regulation Biology of the Ministry of Education, College of Life Science, Beijing Normal University, Beijing, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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