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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
31
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pubmed:dateCreated |
2003-7-28
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pubmed:abstractText |
Upon hepatocyte growth factor stimulation, its receptor c-Met is rapidly internalized via clathrin-coated vesicles and traffics through an early endosomal compartment. We show here that c-Met accumulates progressively in perinuclear compartments, which in part include the Golgi. The c-Met content in the Golgi is principally the newly synthesized precursor form and, to a lesser extent, the internalized, recycling c-Met. By following the trafficking of c-Met inside the cell using a semi-automatic procedure and using inhibition or activation of protein kinase C (PKC) and microtubule depolymerizing agents, we show that PKC positively controls the trans-cytosolic movement of c-Met along microtubules. In parallel to its traffic, internalized c-Met is progressively degraded by a proteasome-sensitive mechanism; the lysosomal pathway does not play a substantial role. Inhibition or promotion of c-Met traffic to the perinuclear compartment does not alter the kinetics of proteasome-dependent c-Met degradation. Thus susceptibility to proteasomal degradation is not a consequence of post-endocytic traffic. The data define a PKC-controlled traffic pathway for c-Met that operates independently of its degradative pathway.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Indoles,
http://linkedlifedata.com/resource/pubmed/chemical/Maleimides,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-met,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/bisindolylmaleimide I
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28921-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12716900-Blotting, Western,
pubmed-meshheading:12716900-Cell Nucleus,
pubmed-meshheading:12716900-Cysteine Endopeptidases,
pubmed-meshheading:12716900-Cytosol,
pubmed-meshheading:12716900-Endocytosis,
pubmed-meshheading:12716900-Endosomes,
pubmed-meshheading:12716900-Enzyme Activation,
pubmed-meshheading:12716900-Enzyme Inhibitors,
pubmed-meshheading:12716900-Fluorescent Antibody Technique,
pubmed-meshheading:12716900-Golgi Apparatus,
pubmed-meshheading:12716900-HeLa Cells,
pubmed-meshheading:12716900-Hepatocyte Growth Factor,
pubmed-meshheading:12716900-Humans,
pubmed-meshheading:12716900-Indoles,
pubmed-meshheading:12716900-Kinetics,
pubmed-meshheading:12716900-Lysosomes,
pubmed-meshheading:12716900-Maleimides,
pubmed-meshheading:12716900-Microscopy, Confocal,
pubmed-meshheading:12716900-Microtubules,
pubmed-meshheading:12716900-Multienzyme Complexes,
pubmed-meshheading:12716900-Proteasome Endopeptidase Complex,
pubmed-meshheading:12716900-Protein Kinase C,
pubmed-meshheading:12716900-Proto-Oncogene Proteins c-met,
pubmed-meshheading:12716900-Recombinant Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Protein kinase C controls microtubule-based traffic but not proteasomal degradation of c-Met.
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pubmed:affiliation |
Protein Phosphorylation Laboratory and Light Microscopy Laboratory, Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom. s.kermorgant@cancer.org.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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