Abstract
The cadherin superfamily protein Fat1 is known to interact with the EVH1 domain of mammalian Ena/VASP. Here we demonstrate that: (i) the scaffolding proteins Homer-3 and Homer-1 also interact with the EVH1 binding site of hFat1 in vitro, and (ii) binding of Homer-3 and Mena to hFat1 is mutually competitive. Endogenous Fat1 binds to immobilised Homer-3 and endogenous Homer-3 binds to immobilised Fat1. Both, endogenous and over-expressed Fat1 exhibit co-localisation with Homer-3 in cellular protrusions and at the plasma membrane of HeLa cells. As Homer proteins and Fat1 have been both linked to psychic disorders, their interaction may be of patho-physiological importance.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cadherins / genetics
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Cadherins / metabolism*
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cell Adhesion Molecules / genetics
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Cell Adhesion Molecules / metabolism
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Cell Membrane / genetics
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Cell Membrane / metabolism
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Gene Expression
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Genetic Linkage
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HeLa Cells
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Homer Scaffolding Proteins
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Humans
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism
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Phosphoproteins / genetics
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Phosphoproteins / metabolism
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Protein Binding / genetics
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Protein Transport / genetics
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Psychotic Disorders / genetics
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Psychotic Disorders / metabolism
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Psychotic Disorders / pathology
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Tumor Suppressor Proteins / genetics
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Tumor Suppressor Proteins / metabolism*
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Vasodilator-Stimulated Phosphoprotein
Substances
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Cadherins
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Carrier Proteins
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Cell Adhesion Molecules
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FAT1 protein, human
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Homer Scaffolding Proteins
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Microfilament Proteins
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Phosphoproteins
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Tumor Suppressor Proteins
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Vasodilator-Stimulated Phosphoprotein