Calcium dependence of the binding of synexin to isolated chromaffin granules

Creutz, Carl E.; Sterner, David C.

doi:10.1016/0006-291x(83)91635-2

Cited by 48 publications

(10 citation statements)

References 13 publications

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“…Synexin was originally isolated as the active principle that promoted adrenal medullary chromaffin granule aggregation when the granules were incubated with crude cytosolic extracts (1). Synexin appeared to act as a glue in this process, rather than as an enzyme that catalysed changes in the membrane surface, as the synexin was found to bind to the chromaffin granules at 5 to 10 pFM calcium (3). However, half-maximal amounts of chromaffin granule aggregation by synexin required more calcium, on the order of 200 p.M (1).…”

Section: Membrane Fusion Mediated By the Annexinsmentioning

confidence: 99%

The Annexins and Exocytosis

Creutz

1992

Science

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538

316

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The annexins are a group of homologous proteins that bind phospholipids in the presence of calcium. They may provide a major pathway for communication between cellular membranes and their cytoplasmic environment. Annexins have a characteristic "bivalent" activity in the sense that they can draw two membranes together when activated by calcium. This has led to the hypothesis that certain members of this protein family may initiate contact and fusion between a secretory vesicle membrane and the plasma membrane during the process of exocytosis.

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Section: Membrane Fusion Mediated By the Annexinsmentioning

confidence: 99%

The Annexins and Exocytosis

Creutz

1992

Science

Self Cite

538

316

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“…Synexin, now known as human annexin A7, was the first member of the family whose Ca 2? -and membrane-binding properties were extensively studied [11]. Its discovery was followed by annexins A1 and A2 (then called lipocortin and calpactin), identified as substrates of Src and EGF protein kinases [12,13].…”

Section: Introductionmentioning

confidence: 99%

The annexins: spatial and temporal coordination of signaling events during cellular stress

Monastyrskaya

Babiychuk

Draeger

2009

Cell. Mol. Life Sci.

124

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Annexins are a family of structurally related, Ca2+-sensitive proteins that bind to negatively charged phospholipids and establish specific interactions with other lipids and lipid microdomains. They are present in all eukaryotic cells and share a common folding motif, the "annexin core", which incorporates Ca2+- and membrane-binding sites. Annexins participate in a variety of intracellular processes, ranging from the regulation of membrane dynamics to cell migration, proliferation, and apoptosis. Here we focus on the role of annexins in cellular signaling during stress. A chronic stress response triggers the activation of different intracellular pathways, resulting in profound changes in Ca2+ and pH homeostasis and the production of lipid second messengers. We review the latest data on how these changes are sensed by the annexins, which have the ability to simultaneously interact with specific lipid and protein moieties at the plasma membrane, contributing to stress adaptation via regulation of various signaling pathways.

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“…One fruitful approach to this problem has been to study proteins such as synexin, which fuse certain natural and artificial membranes in a calciumdependent manner (2)(3)(4)(5)(6)(7)(8)(9)(10)(11). Recently, bovine synexin has been shown to generate classical capacitative gating currents in isolated acidic phospholipid bilayers (12) and to exhibit exquisitely selective, voltage-sensitive calcium channel activity in similar membranes (13).…”

mentioning

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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Calcium dependence of the binding of synexin to isolated chromaffin granules

Cited by 48 publications

References 13 publications

The Annexins and Exocytosis

The Annexins and Exocytosis

The annexins: spatial and temporal coordination of signaling events during cellular stress

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

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