The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.

Sarafian, Tristan; Pradel, Louise‐Anne; Henry, Jean‐Pierre; Aunis, Dominique; Bader, Marie‐France

doi:10.1083/jcb.114.6.1135

Cited by 185 publications

(127 citation statements)

References 50 publications

(65 reference statements)

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“…A possible candidate is annexin II (calpactin I), which has been shown to be necessary for exocytosis in the permeabilized bovine adrenal chromaffin cell (Ali et al, 1989). Pretreatment of chromaffin cells with PMA leads to an increase in membrane bound annexin II, retarding its loss on permeabilization with digitonin (Sarafian et al, 1991). A similar mechanism may exist in pancreatic acinar cells.…”

Section: Discussionmentioning

confidence: 99%

Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini

O’Sullivan

Jamieson

1992

Biochemical Journal

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The effect of protein kinase C (PKC) on amylase discharge from streptolysin-O-permeabilized rat pancreatic acini was investigated. Addition of phorbol 12-myristate 13-acetate (PMA) to permeabilized cells potentiated Ca2+-stimulated release, but had no effect on discharge at non-stimulatory Ca2+ concentrations. PMA markedly shifted the Ca2+-concentration-dependence of amylase discharge to the left, by enhancing the time over which the permeabilized cells release. This effect was inhibited by both staurosporine and PKC-19-31-amide peptide inhibitor, indicating that the effect of PMA was due to its action on PKC. Staurosporine also partially inhibited amylase release at the optimal concentration of Ca2+; this effect was not replicated by the more specific PKC-19-3 1-amide peptide inhibitor and may be due to an effect on another second-messenger system. PKC appears to be an important modulator of release in pancreatic acini, but its activation is not an absolute requirement for Ca2+-dependent amylase discharge.

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Section: Discussionmentioning

confidence: 99%

Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini

O’Sullivan

Jamieson

1992

Biochemical Journal

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“…[34][35][36], including the trafficking of vesicles. In particular, later steps in the Ca 2ϩ -regulated pathway of secretion in chromaffin cells and the peripheral positioning of early endosomes in polarized epithelial cells appear to be affected by annexin II (19). Recently, p11 light chain was shown to be the critical component involved in the plasma membrane translocation of NA V 1.8, a subunit of the tetrodotoxin-resistant sodium channel found in sensory neurones (37).…”

Section: Discussionmentioning

confidence: 99%

“…p11 is the light chain component of the Calpactin complex, in which two heavy chains (annexin II) and two light chains (p11) interact to form the functional tetramer that is important for many cellular processes, including Ca 2ϩ -dependent exocytosis and the correct trafficking of proteins out of the cell (19)(20)(21)(22). In addition to interaction with p11, we show that NS3 also interacts with VP2, the outermost protein of the virion, suggesting that NS3 may mediate an interaction between assembled virions and the host cell export machinery.…”

mentioning

confidence: 99%

The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release

Beaton

Rodrı́guez

Reddy

et al. 2002

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

111

120

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Bluetongue virus, an arbovirus of the Orbivirus genus, infects and replicates in both insect and mammalian cells. However, the cytopathic effect (cpe) on each host is very different. Mammalian cells show substantial cpe, most likely a result of the mechanism of virus release, whereas insect cells show little cpe and appear to release virus without cell lysis. Expression analysis of each infected cell type shows one protein, the nonstructural (NS) protein NS3, to be differentially expressed in the different cell types, suggesting it may act in the virus egress pathway. The molecular basis of such an interaction, however, has never been clear. Here, by using yeast two-hybrid analysis, we show that NS3 interacts with a cellular protein p11 (calpactin light chain), part of the annexin II complex that is involved in exocytosis. We map the NS3 region of interaction with p11 to a 13-residue peptide found at the N terminus of the protein and show it effectively competes with p36 (annexin II heavy chain) for p11 ligand binding. Further, we show that the C-terminal domain of NS3 interacts with VP2, the outermost protein of the fully assembled virus particle, suggesting that NS3 forms a bridging molecule that draws assembled virus into contact with the cellular export machinery. Our data describe the first host protein involvement in orbivirus egress and provide new insights into understanding arbovirus interactions with their hosts.I nsect-borne arboviruses (arthropod-borne viruses), such as members of genus Orbivirus, are vectored to vertebrate species by arthropod species (e.g., gnats, mosquitoes, and ticks) and replicate in both hosts. However, whereas in vertebrate host cells these viruses cause severe cell damage, infections of insect cells are often inapparent. Bluetongue virus (BTV), the prototype virus of the genus Orbivirus, is transmitted by Culicoides spp., causing a disease of economical importance in the vertebrate hosts (ruminants) in many parts of the world. Other orbiviruses (14 serogroups within the genus, including African horse sickness virus and Epizootic hemorrhagic disease virus of deer) infect a variety of vertebrates, including humans, often causing severe diseases (1).Unlike the other arboviruses, BTV and other orbiviruses are nonenveloped and lack the glycosylated proteins known to facilitate both virus entry and exit processes. Consequently, orbiviruses are released from the infected cells predominantly by cell lysis (2, 3). However, BTV causes less severe cytopathic effects in insect vector cells despite highly efficient virus replication (4). BTV release from vector cells is nonlytic, and the virus particles leave the infected cell by passage, either individually or in groups, through a locally disrupted plasma membrane (5). However, the exact mechanism of cell-to-cell spread by the virus is not clear, and how the virus controls differential egress in insect and mammalian cells is one of the most intriguing aspects of BTV biology.BTV virions are architecturally complex icosahedral structures c...

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“…This protein can partially restore Ca2+-dependent secretory activity in digitonin/SLOpermeabilized chromaffin cells, and annexin II can aggregate chromaffin granules at Ca2+ concentrations in the ,tM range (Ali et al, 1989;Drust and Creutz, 1988;Sarafian et al, 1991;Chasserot-Golaz et al, 1996). In the endocytic pathway, immunoelectron microscopic studies have shown that annexin II is associated with plasma membrane and early endosomes of BHK cells and with the apical and basolateral plasma membranes and early endosomes of polarized MDCK cells (Harder and Gerke, 1993).…”

Section: Introductionmentioning

confidence: 99%

Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol.

Harder

Kellner

Parton

et al. 1997

MBoC

197

164

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Annexin II is an abundant protein which is present in the cytosol and on the cytoplasmic face of plasma membrane and early endosomes. It is generally believed that this association occurs via Ca2+-dependent binding to lipids, a mechanism typical for the annexin protein family. Although previous studies have shown that annexin II is involved in early endosome dynamics and organization, the precise biological role of the protein is unknown. In this study, we found that approximately 50% of the total cellular annexin was associated with membranes in a Ca2+-independent manner. This binding was extremely tight, since it resisted high salt and, to some extent, high pH treatments. We found, however, that membrane-associated annexin II could be quantitatively released by low concentrations of the cholesterol-sequestering agents filipin and digitonin. Both treatments released an identical and limited set of proteins but had no effects on other membrane-associated proteins. Among the released proteins, we identified, in addition to annexin II itself, the cortical cytoskeletal proteins a-actinin, ezrin and moesin, and membrane-associated actin. Our biochemical and immunological observations indicate that these proteins are part of a complex containing annexin II and that stability of the complex is sensitive to cholesterol sequestering agents. Since annexin II is tightly membrane-associated in a cholesterol-dependent manner, and since it seems to interact physically with elements of the cortical actin cytoskeleton, we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton.

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The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.

Cited by 185 publications

References 50 publications

Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini

Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini

The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release

Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol.

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