rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2004-4-12
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pubmed:databankReference |
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pubmed:abstractText |
Little is known about the specific signaling roles of Rap2, a Ras family small GTP-binding protein. In a search for novel Rap2-interacting proteins by the yeast two-hybrid system, we isolated isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4), a previously described but uncharacterized isoform. Other isoforms of MAP4K4 in humans and mice are known as hematopoietic progenitor kinase (HPK)/germinal center kinase (GCK)-like kinase and Nck-interacting kinase, respectively. MAP4K4 belongs to the STE20 group of protein kinases and regulates c-Jun N-terminal kinase (JNK). MAP4K4 interacted with Rap2 through its C-terminal citron homology domain but did not interact with Rap1 or Ras. Interaction with Rap2 required the intact effector region of Rap2. MAP4K4 interacted preferentially with GTP-bound Rap2 over GDP-bound Rap2 in vitro. In cultured cells, MAP4K4 colocalized with Rap2, while a mutant MAP4K4 lacking the citron homology domain failed to do so. Furthermore, Rap2 enhanced MAP4K4-induced activation of JNK. These results suggest that MAP4K4 is a putative effector of Rap2 mediating the activation of JNK by Rap2.
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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/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/MAP4K4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RAP2A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Rap2a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/rap GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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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 |
16
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15711-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14966141-Animals,
pubmed-meshheading:14966141-Enzyme Activation,
pubmed-meshheading:14966141-Humans,
pubmed-meshheading:14966141-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:14966141-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:14966141-Mice,
pubmed-meshheading:14966141-Mitogen-Activated Protein Kinases,
pubmed-meshheading:14966141-Molecular Sequence Data,
pubmed-meshheading:14966141-Mutation,
pubmed-meshheading:14966141-NIH 3T3 Cells,
pubmed-meshheading:14966141-Protein Isoforms,
pubmed-meshheading:14966141-Protein Structure, Tertiary,
pubmed-meshheading:14966141-Protein-Serine-Threonine Kinases,
pubmed-meshheading:14966141-Signal Transduction,
pubmed-meshheading:14966141-Substrate Specificity,
pubmed-meshheading:14966141-rap GTP-Binding Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase.
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pubmed:affiliation |
Division of Cell Biology, Graduate School of Medicine, Faculty of Medicine, University of the Ryukyus, 207 Uehara, Nishihara-cho, Okinawa 903-0215, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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