SH3P7/mAbp1 deficiency leads to tissue and behavioral abnormalities and impaired vesicle transport
Identifieur interne : 000924 ( Main/Exploration ); précédent : 000923; suivant : 000925SH3P7/mAbp1 deficiency leads to tissue and behavioral abnormalities and impaired vesicle transport
Auteurs : Sabine Connert [Allemagne] ; Simone Wienand [Allemagne] ; Cora Thiel [Allemagne] ; Maria Krikunova [Allemagne] ; Nataliya Glyvuk [Allemagne] ; Yaroslav Tsytsyura [Allemagne] ; Denise Hilfiker-Kleiner [Allemagne] ; Jörg W. Bartsch [Allemagne] ; Jürgen Klingauf [Allemagne] ; Jürgen Wienands [Allemagne]Source :
- The EMBO Journal [ 0261-4189 ] ; 2006-04-19.
English descriptors
- Teeft :
- Abnormality, Abp1, Actin, Actin cytoskeleton, Adaptor, Allele, Biol, Biol cell, Biol chem, Biology organization, Boutons, Camilli, Cell biol, Clathrin, Connert, Cytoskeleton, Drubin, Dynamin, Dynamin1, Embo, Embo journal, Endocytic, Endocytosis, Error bars, Exon, Female mabp1, Gottingen, Hip1r, Hippocampal, Hippocampal neurons, Internalization, Kessels, Kinase, Kinetics, Mabp1, Mabp1 symptoms, Male mabp1, Mouse, Mutant, Neuron, Presynaptic, Receptor, Recycling, Repriming, Rotarod, Scale bars, Ssion, Standard deviations, Synapse, Synaptic, Synaptic boutons, Synaptic vesicle recycling, Synaptic vesicles, Synaptophysin, Synaptophysin1, Transferrin, Uorescence, Uorescence intensities, Vesicle.
Abstract
The intracellular adaptor protein SH3P7 is the mammalian ortholog of yeast actin‐binding protein 1 and thus alternatively named as mAbp1 (or HIP55). Structural properties, biochemical analysis of its interaction partners and siRNA studies implicated mAbp1 as an accessory protein in clathrin‐mediated endocytosis (CME). Here, we describe the generation and characterization of mice deficient for SH3P7/mAbp1 owing to targeted gene disruption in embryonic stem cells. Mutant animals are viable and fertile without obvious deficits during the first weeks of life. Abnormal structure and function of organs including the spleen, heart, and lung is observed at about 3 months of age in both heterozygous and homozygous mouse mutants. A moderate reduction of both receptor‐mediated and synaptic endocytosis is observed in embryonic fibroblasts and in synapses of hippocampal neurons, respectively. Recycling of synaptic vesicles in hippocampal boutons is severely impaired and delayed four‐fold. The presynaptic defect of SH3P7/mAbp1 mouse mutants is associated with their constricted physical capabilities and disturbed neuromotoric behaviour. Our data reveal a nonredundant role of SH3P7/mAbp1 in CME and places its function downstream of vesicle fission.
Url:
DOI: 10.1038/sj.emboj.7601053
Affiliations:
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<term>Hippocampal neurons</term>
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<term>Kessels</term>
<term>Kinase</term>
<term>Kinetics</term>
<term>Mabp1</term>
<term>Mabp1 symptoms</term>
<term>Male mabp1</term>
<term>Mouse</term>
<term>Mutant</term>
<term>Neuron</term>
<term>Presynaptic</term>
<term>Receptor</term>
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<term>Repriming</term>
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<term>Standard deviations</term>
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<term>Synaptic vesicles</term>
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<front><div type="abstract">The intracellular adaptor protein SH3P7 is the mammalian ortholog of yeast actin‐binding protein 1 and thus alternatively named as mAbp1 (or HIP55). Structural properties, biochemical analysis of its interaction partners and siRNA studies implicated mAbp1 as an accessory protein in clathrin‐mediated endocytosis (CME). Here, we describe the generation and characterization of mice deficient for SH3P7/mAbp1 owing to targeted gene disruption in embryonic stem cells. Mutant animals are viable and fertile without obvious deficits during the first weeks of life. Abnormal structure and function of organs including the spleen, heart, and lung is observed at about 3 months of age in both heterozygous and homozygous mouse mutants. A moderate reduction of both receptor‐mediated and synaptic endocytosis is observed in embryonic fibroblasts and in synapses of hippocampal neurons, respectively. Recycling of synaptic vesicles in hippocampal boutons is severely impaired and delayed four‐fold. The presynaptic defect of SH3P7/mAbp1 mouse mutants is associated with their constricted physical capabilities and disturbed neuromotoric behaviour. Our data reveal a nonredundant role of SH3P7/mAbp1 in CME and places its function downstream of vesicle fission.</div>
</front>
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<name sortKey="Klingauf, Jurgen" sort="Klingauf, Jurgen" uniqKey="Klingauf J" first="Jürgen" last="Klingauf">Jürgen Klingauf</name>
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<name sortKey="Wienands, Jurgen" sort="Wienands, Jurgen" uniqKey="Wienands J" first="Jürgen" last="Wienands">Jürgen Wienands</name>
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