Structure and functional relevance of the Slit2 homodimerization domain
Copyright policy )Structure and functional relevance of the Slit2 homodimerization domain
Slit proteins are secreted ligands that interact with the Roundabout (Robo) receptors to provide important guidance cues in neuronal and vascular development. Slit–Robo signalling is mediated by an interaction between the second Slit domain and the first Robo domain, as well as being dependent on heparan sulphate. In an effort to understand the role of the other Slit domains in signalling, we determined the crystal structure of the fourth Slit2 domain (D4) and examined the effects of various Slit2 constructs on chick retinal ganglion cell axons. Slit2 D4 forms a homodimer using the conserved residues on its concave face, and can also bind to heparan sulphate. We observed that Slit2 D4 frequently results in growth cones with collapsed lamellipodia and that this effect can be inhibited by exogenously added heparan sulphate. Our results show that Slit2 D4–heparan sulphate binding contributes to a Slit–Robo signalling mechanism more intricate than previously thought.
MESH: Extracellular Matrix Proteins, Models, Molecular, 570, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Scientific Report, Static Electricity, Nerve Tissue Proteins, Slit Homolog 2 Protein, Structure-Activity Relationship, MESH: Structure-Activity Relationship, MESH: Heparitin Sulfate, MESH: Models, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, MESH: Sequence Homology, MESH: Nerve Tissue Proteins, MESH: Intercellular Signaling Peptides and Proteins, Molecular Biology, MESH: Static Electricity, Conserved Sequence, info:eu-repo/classification/ddc/570, Extracellular Matrix Proteins, MESH: Conserved Sequence, MESH: Humans, Sequence Homology, Amino Acid, biology, MESH: Protein Multimerization, MESH: Decorin, Molecular, Life sciences, Protein Structure, Tertiary, Amino Acid, MESH: Protein Structure, MESH: Proteoglycans, Intercellular Signaling Peptides and Proteins, Proteoglycans, ddc:570, Heparitin Sulfate, Decorin, Protein Multimerization, Tertiary
MESH: Extracellular Matrix Proteins, Models, Molecular, 570, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Scientific Report, Static Electricity, Nerve Tissue Proteins, Slit Homolog 2 Protein, Structure-Activity Relationship, MESH: Structure-Activity Relationship, MESH: Heparitin Sulfate, MESH: Models, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, MESH: Sequence Homology, MESH: Nerve Tissue Proteins, MESH: Intercellular Signaling Peptides and Proteins, Molecular Biology, MESH: Static Electricity, Conserved Sequence, info:eu-repo/classification/ddc/570, Extracellular Matrix Proteins, MESH: Conserved Sequence, MESH: Humans, Sequence Homology, Amino Acid, biology, MESH: Protein Multimerization, MESH: Decorin, Molecular, Life sciences, Protein Structure, Tertiary, Amino Acid, MESH: Protein Structure, MESH: Proteoglycans, Intercellular Signaling Peptides and Proteins, Proteoglycans, ddc:570, Heparitin Sulfate, Decorin, Protein Multimerization, Tertiary
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