Source:http://linkedlifedata.com/resource/pubmed/id/10608885
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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001613,
umls-concept:C0007776,
umls-concept:C0022655,
umls-concept:C0024880,
umls-concept:C0036536,
umls-concept:C0036537,
umls-concept:C0332287,
umls-concept:C1412517,
umls-concept:C1423613,
umls-concept:C1622186,
umls-concept:C1707798,
umls-concept:C1720675,
umls-concept:C1880352,
umls-concept:C2587213
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pubmed:issue |
53
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pubmed:dateCreated |
2000-2-8
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pubmed:abstractText |
Localized disassembly of cortical F-actin has long been considered necessary for facilitation of exocytosis. Exposure of permeabilized mast cells to calcium/ATP induces cortical F-actin disassembly (calmodulin-dependent) and secretion (calmodulin-independent). The delay in the onset of secretion is characteristic for the calcium/ATP response and is abolished by GTP. Here we report that a constitutively active mutant of Rho (V14RhoA) enhanced both secretion and cortical F-actin disassembly. In addition, V14RhoA mimicked GTP by abolishing the delay in secretion. Inhibition of Rho by C3 transferase prevented both secretion ( approximately 80%) and F-actin disassembly (approximately 20%). Thus, both Rho GTPase and calcium/calmodulin contribute to the control of cortical F-actin disassembly. Stabilization of actin filaments by high concentrations of phalloidin or by a calmodulin-inhibitory peptide (based on the calmodulin-binding domain of myosin light chain kinase) did not affect the extent of secretion or the secretion-enhancing effects of V14RhoA. These results further support the existence of divergent, Rho-dependent, pathways regulating actin and exocytosis. Furthermore, compound Y-27632, a specific inhibitor of Rho-associated protein kinase (p160(ROCK)), attenuated the Rho-induced loss of cortical F-actin without affecting secretion. A model is presented in which Rho regulates secretion and cortical F-actin in a manner dependent on and/or synergistic with calcium.
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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/Amides,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridines,
http://linkedlifedata.com/resource/pubmed/chemical/Y 27632,
http://linkedlifedata.com/resource/pubmed/chemical/rho-Associated Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
38140-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10608885-Actins,
pubmed-meshheading:10608885-Amides,
pubmed-meshheading:10608885-Amino Acid Sequence,
pubmed-meshheading:10608885-Animals,
pubmed-meshheading:10608885-Calcium,
pubmed-meshheading:10608885-Enzyme Inhibitors,
pubmed-meshheading:10608885-GTP-Binding Proteins,
pubmed-meshheading:10608885-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10608885-Mast Cells,
pubmed-meshheading:10608885-Molecular Sequence Data,
pubmed-meshheading:10608885-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10608885-Pyridines,
pubmed-meshheading:10608885-Rats,
pubmed-meshheading:10608885-rho-Associated Kinases
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pubmed:year |
1999
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pubmed:articleTitle |
Rho controls cortical F-actin disassembly in addition to, but independently of, secretion in mast cells.
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pubmed:affiliation |
Physiology Department, University College London, University Street, London WC1E 6JJ, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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