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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0109317,
umls-concept:C0752312,
umls-concept:C1150579,
umls-concept:C1166758,
umls-concept:C1179132,
umls-concept:C1332768,
umls-concept:C1333340,
umls-concept:C1334325,
umls-concept:C1334474,
umls-concept:C1364078,
umls-concept:C1366882,
umls-concept:C1370600,
umls-concept:C1521840,
umls-concept:C1704803,
umls-concept:C1705767,
umls-concept:C1705791,
umls-concept:C1825781
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pubmed:issue |
Pt 10
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pubmed:dateCreated |
2004-4-19
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pubmed:abstractText |
The identification and characterization of scaffold and targeting proteins of the ERK/MAP kinase pathway is important to understand the function and intracellular organization of this pathway. The F-actin binding protein leukocyte-specific protein 1 (LSP1) binds to PKCbetaI and expression of B-LSP1, an LSP1 truncate containing the PKCbetaI binding residues, inhibits anti-IgM-induced translocation of PKCbetaI to the plasma membrane and anti-IgM-induced activation of ERK2. To understand the role of LSP1 in the regulation of PKCbetaI-dependent ERK2 activation, we investigated whether LSP1 interacts with ERK/MAP kinase pathway components and targets these proteins to the actin cytoskeleton. We show that LSP1 associates with the ERK scaffold protein KSR and with MEK1 and ERK2. LSP1-associated MEK1 is activated by anti-IgM treatment and this activation is inhibited by expression of B-LSP1, suggesting that the activation of LSP1-associated MEK1 is PKCbetaI dependent. Confocal microscopy showed that LSP1 targets KSR, MEK1 and ERK2 to peripheral actin filaments. Thus our data show that LSP1 is a cytoskeletal targeting protein for the ERK/MAP kinase pathway and support a model in which MEK1 and ERK2 are organized in a cytoskeletal signaling complex together with KSR, PKCbetaI and LSP1 and are activated by anti-IgM in a PKCbetaI-dependent manner.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/F-actin-binding proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/LST1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
117
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2151-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15090600-Actins,
pubmed-meshheading:15090600-Blood Proteins,
pubmed-meshheading:15090600-Carrier Proteins,
pubmed-meshheading:15090600-Cell Line,
pubmed-meshheading:15090600-Cell Line, Tumor,
pubmed-meshheading:15090600-Cell Membrane,
pubmed-meshheading:15090600-Cytoskeleton,
pubmed-meshheading:15090600-Glutathione Transferase,
pubmed-meshheading:15090600-Humans,
pubmed-meshheading:15090600-Immunoglobulin M,
pubmed-meshheading:15090600-Immunoprecipitation,
pubmed-meshheading:15090600-Leukocytes,
pubmed-meshheading:15090600-Lymphoma, B-Cell,
pubmed-meshheading:15090600-MAP Kinase Kinase 1,
pubmed-meshheading:15090600-MAP Kinase Signaling System,
pubmed-meshheading:15090600-Membrane Proteins,
pubmed-meshheading:15090600-Microfilament Proteins,
pubmed-meshheading:15090600-Microscopy, Confocal,
pubmed-meshheading:15090600-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:15090600-Protein Binding,
pubmed-meshheading:15090600-Time Factors,
pubmed-meshheading:15090600-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
Leukocyte-specific protein 1 targets the ERK/MAP kinase scaffold protein KSR and MEK1 and ERK2 to the actin cytoskeleton.
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pubmed:affiliation |
Cell Biology Programme, The Hospital for Sick Children Research Institute, Toronto, Ontario, M5G 1X8, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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