Endophilin regulates JNK activation through its interaction with the germinal center kinase-like kinase
| Autor: | Annie Angers, Valerie Legendre-Guillemin, Antoine R. Ramjaun, Peter S. McPherson, Xin-Kang Tong |
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| Rok vydání: | 2001 |
| Předmět: |
Recombinant Fusion Proteins
Molecular Sequence Data Biology Protein Serine-Threonine Kinases Endocytosis Biochemistry SH3 domain Homology (biology) src Homology Domains Consensus Sequence Animals Humans Amino Acid Sequence Molecular Biology Adaptor Proteins Signal Transducing Gene Library chemistry.chemical_classification Binding Sites Base Sequence Sequence Homology Amino Acid Kinase Reverse Transcriptase Polymerase Chain Reaction JNK Mitogen-Activated Protein Kinases Germinal center Brain Cell Biology In vitro Cell biology Rats Enzyme Activation Enzyme chemistry Mitogen-Activated Protein Kinases Carrier Proteins Sequence Alignment Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | The Journal of biological chemistry. 276(31) |
| ISSN: | 0021-9258 |
| Popis: | The endophilin family of proteins function in clathrin-mediated endocytosis. Here, we have identified and cloned the rat germinal center kinase-like kinase (rGLK), a member of the GCK (germinal center kinase) family of c-Jun N-terminal kinase (JNK) activating enzymes, as a novel endophilin I-binding partner. The interaction occurs both in vitro and in cells and is mediated by the Src homology 3 domain of endophilin I and a region of rGLK containing the endophilin consensus-binding sequence PPRPPPPR. Overlay analysis of rat brain extracts demonstrates that endophilin I is a major Src homology 3 domain-binding partner for rGLK. Overexpression of full-length endophilin I activates rGLK-mediated JNK activation, whereas N- and C-terminal fragments of endophilin I block JNK activation. Thus, endophilin I appears to have a novel function in JNK activation. |
| Databáze: | OpenAIRE |
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