Pattern of repeating aromatic residues in synexin. Similarity to the cytoplasmic domain of synaptophysin

Creutz, Carl E.; Snyder, Sandra L.; Husted, Lisa D.; Beggerly, Linda K.; Fox, Jay W.

doi:10.1016/s0006-291x(88)80426-1

Cited by 20 publications

(8 citation statements)

References 18 publications

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“…Consistently, the basis for the difference in size of the two classes rests on the fact that the larger class contains 893 bp of unique non-coding sequence after the 311 bp 3' noncoding region found in both groups. The longer group II cDNAs also have the expected two polyadenylation signals, (Creutz et al, 1988;Burnsetal, 1989). The location of a-helices in the repeating units are boxed and indicated as A, B, C, D and E. Arrows indicate amino acid differences between mouse and human synexin.…”

Section: Discussionmentioning

confidence: 98%

Mouse synexin (annexin VII) polymorphisms and a phylogenetic comparison with other synexins

Zhang-Keck

Burns

Pollard

1993

Biochemical Journal

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Two sets of cDNAs encoding mouse synexin were isolated from a liver cDNA library and sequenced. The coding regions of synexin clones show 99% identity. By contrast, the two mouse synexin cDNAs differ in a number of ways in both 5′ and 3′ non-coding regions. The two sets of cDNA encode a polypeptide of 463 amino acid residues which has a deduced molecular mass of 50 kDa. The amino acid sequence of mouse synexin shows a high degree of similarity to both the unique N-terminal domain and the highly conserved C-terminal domain of previously cloned human synexin. Northern-blot analysis using mouse liver polyadenylated RNA revealed two transcripts of 1.8 kb and 2.6 kb, corresponding to group I and group II respectively. Further hybridization analysis using specific sequences from each set of clones showed that the two sizes of mRNAs differ in the length of the 3′ non-coding region which corresponded to the cDNAs. Both mouse liver synexin and recombinant mouse synexin expressed in Escherichia coli reacted after Western-blot analysis with a goat antibody against bovine synexin. Only in the larger group-II cDNAs do we find point mutations leading to amino acid replacements of Ser to Ala at residue 145 in the unique N-terminal domain, and of Ala to Gly at residue 304 in the transition zone between repeats II and III. We conclude from a comparison of mouse, human and Dictyostelium synexins that changes occur predominantly in the hydrophobic N-terminal domain, or, in the C-terminal region at the ends of some predicted alpha-helices, on the hydrophobic face of the amphipathic C-helices, and within a lengthy non-helical domain connecting major repeats II and III.

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Section: Discussionmentioning

confidence: 98%

Mouse synexin (annexin VII) polymorphisms and a phylogenetic comparison with other synexins

Zhang-Keck

Burns

Pollard

1993

Biochemical Journal

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“…This segment is also highly enriched in glycine, tyrosine, and proline and is largely /3-turn and /8-sheet. ,,zM,,,,,,,,tt,,,,,,,,,,,/,,z,, (23,35) within all regions (overlined in Fig. 3), which contains invariant glycine and arginine.…”

Section: Discussionmentioning

confidence: 99%

Calcium channel activity of purified human synexin and structure of the human synexin gene.

Burns

Magendzo

Shirvan

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

135

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Synexin is a calcium-dependent membrane binding protein that not only fuses membranes but also acts as a voltage-dependent calcium channel. We have isolated and sequenced a set ofoverlapping cDNA clones for human synexin. The derived amino acid sequence of synexin reveals strong homology in the C-terminal domain with a previously identified class of calcium-dependent membrane binding proteins. (18,19). cDNA inserts of the three positive recombinants or restriction fragments of the largest cDNA (L4a) were subcloned into M13 for DNA sequencing with M13-or synexinspecific primers (20). Specific oligonucleotide or cDNA probes were used to screen additional cDNA libraries: retina from Jeremy Nathans (Genentech) (Fig. 2); B-cell, adrenal, and lung from Clontech; and fibroblast from H. Okayama (National Institutes of Health) (data not shown) (20).Single Channel Current Measurements. Calcium channel activity of human synexin was measured by methods previously described (refs. 13, 21; Fig. 1 B and C). Briefly, bilayers of phosphatidylserine (PtdSer) or phosphatidylinositol (PtdIns) (Avanti Polar Lipids) were prepared at the tips of patch pipets by a double dip method. Upon forming the bilayer the open tip resistance rose from 15-20 MQ to 3-5 GQl, and channel activity was acquired only after addition of synexin to the bath. The compositions of the various solutions are stated either in the legend to Fig. 1 or in the text.

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“…The other members of the family include endonexin II (E2 [36,19]); lipocortin I (L1 [44]), calpactin heavy chain/ p36 (C1 [12, 18, 21, 35]), protein II (p2 [45]), and and 13 times, respectively. Although this N-terminal region has slight similarities to collagen, glutinin, keratin, synaptophysin and gliadin [8], the function of this hydrophobic domain remains to be determined.…”

Section: Synexin Is a Member Of The Annexin Gene Family Of Calcium-dementioning

confidence: 99%

Synexin (annexin VII): A cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes

1990

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Pattern of repeating aromatic residues in synexin. Similarity to the cytoplasmic domain of synaptophysin

Cited by 20 publications

References 18 publications

Mouse synexin (annexin VII) polymorphisms and a phylogenetic comparison with other synexins

Mouse synexin (annexin VII) polymorphisms and a phylogenetic comparison with other synexins

Calcium channel activity of purified human synexin and structure of the human synexin gene.

Synexin (annexin VII): A cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes

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