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A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin
Author(s) -
Petrucci Tamara C.,
Mooseker Mark S.,
Morrow Jon S.
Publication year - 1988
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240360104
Subject(s) - phosphoprotein , peptide , biochemistry , villin , actin , biology , synapsin i , chemistry , actin binding protein , phosphopeptide , phosphorylation , actin cytoskeleton , cytoskeleton , synaptic vesicle , vesicle , membrane , cell
Abstract Synapsin I is a neuronal phosphoprotein that can bundle actin filaments in vitro. This activity is under phosphorylation control, and may be related to its putative in vivo role of regulating the clustering and release of small synaptic vesicles. We have compared human and bovine synapsin I by peptide mapping, and have used NTCB (2‐nitro‐5‐thiocyano benzoic acid) cleavage to generate a series of peptide fragments from bovine synapsin I. After chymotryptic digestion, 88% of the tyrosine‐containing fragments appear to be structurally identical in human and bovine synapsin I, as judged by their positions on high‐resolution two‐dimensional peptide maps. The alignment of the NTCB peptides within the parent protein have been determined by peptide mapping, and the ability of these fragments to precipitate with actin bundles has been measured. Only peptides that are derived from regions near the ends of the protein are active. One such 25‐kDa peptide which sediments with actin also cross‐reacts with antibodies to chicken villin, an actin binding and bundling protein derived from the intestinal microvillus. Since in other respects villin appears to be an unrelated protein, these results suggest the possibility that certain actin binding proteins may show immunologic cross‐reactivity due to convergent evolution within the acting binding domain.