A 70 Amino Acid Region within the Semaphorin Domain Activates Specific Cellular Response of Semaphorin Family Members

The semaphorin family contains secreted and transmembrane signaling proteins that function in the nervous, immune, and cardiovascular systems. Chick collapsin-1 is a repellent for specific growth cones. Two other secreted members of the semaphorin family, collapsin-2 and -3, are structurally similar...

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Bibliographic Details
Published in:Neuron (Cambridge, Mass.) Mass.), 1997-09, Vol.19 (3), p.531-537
Main Authors: Koppel, Adam M, Feiner, Leonard, Kobayashi, Hiroaki, Raper, Jonathan A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Avian Proteins
Cell Communication - physiology
Cells, Cultured
Chick Embryo
Conserved Sequence
Gene Expression
Glycoproteins - chemistry
Glycoproteins - genetics
Glycoproteins - metabolism
Nerve Growth Factors - chemistry
Nerve Growth Factors - genetics
Nerve Growth Factors - metabolism
Nerve Tissue Proteins - metabolism
Neuropilin-1
Plasmids
Protein Structure, Tertiary
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Semaphorin-3A
Sensitivity and Specificity
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Summary:The semaphorin family contains secreted and transmembrane signaling proteins that function in the nervous, immune, and cardiovascular systems. Chick collapsin-1 is a repellent for specific growth cones. Two other secreted members of the semaphorin family, collapsin-2 and -3, are structurally similar to collapsin-1 but have different biological activities. Semaphorins contain a 500 amino acid family signature semaphorin domain. We show in this study that (1) the semaphorin domain of collapsin-1 is both necessary and sufficient for biological activity, (2) the semaphorin domain contains a 70 amino acid region that specifies the biological activity of the three family members, and (3) the positively charged carboxy terminus potentiates activity without affecting specificity. We propose that semaphorins interact with their receptors through two independent binding sites: one that mediates the biological response and one that potentiates it.
ISSN:0896-6273
1097-4199
DOI:10.1016/S0896-6273(00)80369-4