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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2004-8-17
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pubmed:abstractText |
Keratins 8 and 18 (K8/18) heteropolymers may regulate cell signaling via the known K18 association with 14-3-3 proteins and 14-3-3 association with Raf-1 kinase. We characterized Raf-keratin-14-3-3 associations and show that Raf associates directly with K8, independent of Raf kinase activity or Ras-Raf interaction, and that K18 is a Raf physiologic substrate. Raf activation during oxidative and toxin exposure in cultured cells and animals disrupt keratin-Raf association in a phosphorylation-dependent manner. Mutational analysis showed that 14-3-3 residues that are essential for Raf binding also regulate 14-3-3-keratin association. Similarly, Raf phosphorylation sites that are important for binding to 14-3-3 are also essential for Raf binding to K8/18. Therefore, keratins may modulate some aspects of Raf signaling under basal conditions via sequestration by K8, akin to Raf-14-3-3 binding. Keratin-bound Raf kinase is released upon Raf hyperphosphorylation and activation during oxidative and other stresses.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-10354017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-10836149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-10887173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-11023985,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-11336675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-11514590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-11709560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-11792552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-11911880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-11917136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-11973607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-1943760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-6186379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-6208369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-7523419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-7529764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-7603573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-7603574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-7979242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-8016101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-8609167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-9153224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-9407108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-9428519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-9438837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-9524113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-9665134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-9823899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15314064-9932491
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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/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Keratins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Polymers,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-raf,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9525
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
479-85
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15314064-14-3-3 Proteins,
pubmed-meshheading:15314064-Animals,
pubmed-meshheading:15314064-Binding Sites,
pubmed-meshheading:15314064-Cell Line,
pubmed-meshheading:15314064-Cell Line, Tumor,
pubmed-meshheading:15314064-Cricetinae,
pubmed-meshheading:15314064-DNA, Complementary,
pubmed-meshheading:15314064-DNA Mutational Analysis,
pubmed-meshheading:15314064-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15314064-Humans,
pubmed-meshheading:15314064-Keratins,
pubmed-meshheading:15314064-Mice,
pubmed-meshheading:15314064-Mice, Transgenic,
pubmed-meshheading:15314064-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:15314064-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:15314064-Mitogen-Activated Protein Kinases,
pubmed-meshheading:15314064-Models, Biological,
pubmed-meshheading:15314064-Mutation,
pubmed-meshheading:15314064-Oxidative Stress,
pubmed-meshheading:15314064-Oxygen,
pubmed-meshheading:15314064-Phosphorylation,
pubmed-meshheading:15314064-Polymers,
pubmed-meshheading:15314064-Precipitin Tests,
pubmed-meshheading:15314064-Protein Binding,
pubmed-meshheading:15314064-Proto-Oncogene Proteins c-raf,
pubmed-meshheading:15314064-Transfection,
pubmed-meshheading:15314064-Tyrosine 3-Monooxygenase
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pubmed:year |
2004
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pubmed:articleTitle |
Raf-1 activation disrupts its binding to keratins during cell stress.
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pubmed:affiliation |
Department of Medicine, VA Palo Alto Medical Center, 3801 Miranda Ave., 154J, Palo Alto, CA 94304, USA.
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