The Roles of Ca2+Dependent Membrane-Binding Proteins in the Regulation and Mechanism of Exocytosis

Creutz, Carl E.; Zaks, William J.; Hamman, Helen C.; Martin, William H.

doi:10.1007/978-1-4757-9598-1_3

Cited by 16 publications

(11 citation statements)

References 52 publications

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“…Mitochondrial annexin VI from bovine liver has the same electrophoretic migration as the form exhibiting the hydrophobic hexapeptide VAAEIL [21]. Its amino acid composition is very similar to those of previously described bovine [18,22,23,24] or human annexins VI [25] and its N-terminus is blocked. Proteolysis ofmitochondrial annexin VI gives rise to peptides identical to those of bovine annexins VI from other sources, as determined by sequence determination [18,25,26].…”

Section: Discussionsupporting

confidence: 66%

“…1, M), only one band could be observed at the level of the upper band of the doublet. Table 1 Comparison of the amino acid composition (mol %) of the 67 kDa protein isolated from bovine liver mitochondria with those of annexins VI isolated from Bovine liver [22,23], bovine brain [24], or bovine aorta [18], and with the amino acid composition calculated from the sequence of the human annexin VI [25]. …”

Section: Demonstration Of the Presence Of Annexin VI In Different Framentioning

confidence: 99%

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Characterization and ultrastructural localization of annexin VI from mitochondria

Rainteau¹,

Mansuelle

Rochat

et al. 1995

FEBS Letters

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Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca2+-dependent manner, has been purified from bovine liver mitochondria and characterized. Moreover, biochemical and immunocytochemical lines of evidence are presented which strongly suggest that annexin VI is closely associated with the cristae in the inner membrane of mitochondria. These findings are consistent with a calcium channel activity of annexin VI in mitochondria.

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Section: Discussionsupporting

confidence: 66%

Section: Demonstration Of the Presence Of Annexin VI In Different Framentioning

confidence: 99%

Characterization and ultrastructural localization of annexin VI from mitochondria

Rainteau¹,

Mansuelle

Rochat

et al. 1995

FEBS Letters

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“…We suggest that endonexin II [ 131, the human placental anticoagulant protein [37,38], chromobindins 5 and 7 [17,26] and the two new proteins reported here represent a fifth group.…”

Section: Characterization Of And'-dependent Phospholipid-binding Propermentioning

confidence: 90%

Isolation and characterization of two novel calcium‐dependent phospholipid‐binding proteins from bovine lung

1988

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Two calcium‐dependent proteins of apparent M r 32000 and 34000 were isolated from bovine lung. Approx. 70 mg/kg of each was obtained. Two‐dimensional gel electrophoresis in the presence of 8 M urea showed their apparent p I values to be 5.1 and 5.0, respectively. Both proteins are related immunologically to calelectrin from Torpedo marmorata. They also have very similar amino acid compositions to calelectrin. Partial sequence information shows that both proteins contain the highly conserved sequence described for the annexins, a new family of calcium‐dependent membrane‐binding proteins. In common with other members of this family, the new proteins bind to acidic phospholipids in a calcium‐dependent manner.

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“…This includes the phosphorylation of a variety of intracellular components as well as of proteins bound to secretory organelle membranes [22] and of cell membrane constituents, such as ion channels [23], ion pumps [24], receptors [25,26], etc. Proteins undergoing dephosphorylation have rarely been thoroughly analyzed.…”

Section: Aspects Pertinent To the Involvement Of Phosphoproteins In Ementioning

confidence: 99%

“…While the identity and role of integral membrane proteins remain poorly understood, membrane-associated proteins could in part be identified (see section 4.2). According to studies with model systems synexin and related proteins were also considered as fusogenic proteins [22,33,34]. Yet, so far, no conclusive proof of the involvement of any of these proteins in membrane fusion regulation in vivo has been presented.…”

Section: Aspects Pertinent To a General Mechanism Of Membrane Fusionmentioning

confidence: 99%

Involvement of a 65 kDa phosphoprotein in the regulation of membrane fusion during exocytosis in Paramecium cells

et al. 1987

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Antisera were raised against a phosphoprotein of 65 kDa (PP65) from Paramecium cells (shown before to be selectively dephosphorylated during synchronous exocytosis) and specified by immunoblotting. By immunofluorescence PP65 has been localized within the cortex, beneath the cell membrane. This corresponds to data obtained by cell fractionation, applying SDS-PAGE autoradiography to cortices prepared from 32p_ prelabeled cells. Antisera against PP65 inhibit exocytosis in vivo (microinjection). Applying anti-PP65 antisera in vitro to cortices we could demonstrate inhibition not only of exocytosis, but also of PP65 dephosphorylation. We conclude that PP65 is involved in the regulation of membrane fusion during exocytosis.

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The Roles of Ca2+Dependent Membrane-Binding Proteins in the Regulation and Mechanism of Exocytosis

Cited by 16 publications

References 52 publications

Characterization and ultrastructural localization of annexin VI from mitochondria

Characterization and ultrastructural localization of annexin VI from mitochondria

Isolation and characterization of two novel calcium‐dependent phospholipid‐binding proteins from bovine lung

Involvement of a 65 kDa phosphoprotein in the regulation of membrane fusion during exocytosis in Paramecium cells

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