Abstract
The adapter 3BP2 is involved in leukocyte signaling downstream Src/Syk-kinases coupled immunoreceptors. Here, we show that 3BP2 directly interacts with the endocytic scaffold protein CIN85 and the actin-binding protein HIP-55. 3BP2 co-localized with CIN85 and HIP-55 in T cell rafts and at the T cell/APC synapse, an active zone of receptors and proteins recycling. A binding region of CIN85 SH3 domains on 3BP2 was mapped to a PVPTPR motif in the first proline-rich region of 3BP2, whereas the C-terminal SH3 domain of HIP-55 bound a more distal proline-rich domain of 3BP2. Together, our data suggest an unexpected role of 3BP2 in endocytic and cytoskeletal regulation through its interaction with CIN85 and HIP-55.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / chemistry
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Adaptor Proteins, Signal Transducing / genetics
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Adaptor Proteins, Signal Transducing / metabolism*
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Amino Acid Motifs
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Amino Acid Sequence
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Binding Sites
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Cell Line
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Cytoskeleton / metabolism
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Endocytosis
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Humans
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In Vitro Techniques
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Jurkat Cells
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Microfilament Proteins / chemistry
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism*
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Models, Biological
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Proline / chemistry
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Protein Binding
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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T-Lymphocytes / metabolism
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Two-Hybrid System Techniques
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src Homology Domains / genetics
Substances
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Adaptor Proteins, Signal Transducing
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DBNL protein, human
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Microfilament Proteins
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Recombinant Proteins
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SH3BP2 protein, human
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SH3KBP1 protein, human
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Proline