Abstract
The immune cell specific protein Fyn-T binding protein (Fyb) has been identified as a target of the Yersinia antiphagocytic effector Yersinia outer protein H (YopH), but its role in macrophages is unknown. By using Fyb domains as bait to screen a mouse lymphoma cDNA library, we identified a novel interaction partner, mammalian actin binding protein 1 (mAbp1). We show that mAbp1 binds the Fyb N-terminal via its C-terminally located src homology 3 domain. The interaction between Fyb and mAbp1 is detected in macrophage lysates and the proteins co-localize with F-actin in the leading edge. Hence, mAbp1 is likely to constitute a downstream effector of Fyb involved in F-actin dynamics.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism
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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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Animals
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Bacterial Outer Membrane Proteins / metabolism
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Cell Line
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Mice
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism*
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Phosphorylation
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Phosphotyrosine / metabolism
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Protein Binding
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Protein Transport
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Protein Tyrosine Phosphatases / metabolism
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-fyn
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Two-Hybrid System Techniques
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src Homology Domains / genetics
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src-Family Kinases / metabolism
Substances
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Actins
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Adaptor Proteins, Signal Transducing
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Bacterial Outer Membrane Proteins
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Dbnl protein, mouse
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Fyb protein, mouse
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Microfilament Proteins
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Proto-Oncogene Proteins
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Phosphotyrosine
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Fyn protein, mouse
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Proto-Oncogene Proteins c-fyn
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src-Family Kinases
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Protein Tyrosine Phosphatases
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yopH protein, Yersinia