Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin (Q24291404)

Regulating synaptic membrane exocytosis 1

GOA release 2020-03-11

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protein-containing complex assembly

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

T Coppola

1

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Romano Regazzi

object named as

R Regazzi

6

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author name string

S Magnin-Luthi

2

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V Perret-Menoud

3

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S Gattesco

4

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G Schiavo

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

31 August 2001

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published in

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volume

276

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page(s)

32756-62

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issue

35

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cites work

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SNARE interactions are not selective. Implications for membrane fusion specificity

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Ca2+ regulates the interaction between synaptotagmin and syntaxin 1.

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Distinct roles of C2A and C2B domains of synaptotagmin in the regulation of exocytosis in adrenal chromaffin cells.

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Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin

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Interaction of the synprint site of N-type Ca2+ channels with the C2B domain of synaptotagmin I.

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Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses

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Rab proteins in regulated exocytosis

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Disruption of Rab3-calmodulin interaction, but not other effector interactions, prevents Rab3 inhibition of exocytosis

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The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion

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Overexpression of Rab3D enhances regulated amylase secretion from pancreatic acini of transgenic mice

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Inhibition of Rab3B expression attenuates Ca(2+)-dependent exocytosis in rat anterior pituitary cells

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t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase

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Identification of Rab6 as an N-ethylmaleimide-sensitive fusion protein-binding protein

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The Rab5 effector EEA1 interacts directly with syntaxin-6

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Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13

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Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion

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The RIM/NIM family of neuronal C2 domain proteins. Interactions with Rab3 and a new class of Src homology 3 domain proteins

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The Rab3-interacting molecule RIM is expressed in pancreatic beta-cells and is implicated in insulin exocytosis.

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cAMP-GEFII is a direct target of cAMP in regulated exocytosis

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Calcium dependence of the rate of exocytosis in a synaptic terminal

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Functional diversity of C2 domains of synaptotagmin family. Mutational analysis of inositol high polyphosphate binding domain.

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Synaptic function modulated by changes in the ratio of synaptotagmin I and IV.

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The GTPase Rab3a negatively controls calcium-dependent exocytosis in neuroendocrine cells.

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Synaptotagmin is an inositol polyphosphate binding protein: isolation and characterization as an Ins 1,3,4,5-P4 binding protein

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Location of the membrane-docking face on the Ca2+-activated C2 domain of cytosolic phospholipase A2

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Identifiers

DOI

10.1074/JBC.M100929200

1 reference

Consolidated OpenCitations Corpus – April 2017

4081393

4081393

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference