pH-Dependent association of chromogranin A with secretory vesicle membrane and a putative membrane binding region of chromogranin A

Biochemistry ◽  
1993 ◽  
Vol 32 (32) ◽  
pp. 8213-8219 ◽  
Author(s):  
Seung Hyun Yoo
Keyword(s):  
Chromogranin A ◽  
Membrane Binding ◽  
Secretory Vesicle ◽  
Binding Region ◽  
Vesicle Membrane ◽  
Ph Dependent

scholarly journals Kiss-and-Coat and Compartment Mixing: Coupling Exocytosis to Signal Generation and Local Actin Assembly

2006 ◽  
Vol 17 (4) ◽  
pp. 1495-1502 ◽  
Author(s):  
Anna M. Sokac ◽  
William M. Bement
Keyword(s):  
Cell Types ◽  
Secretory Vesicle ◽  
Signal Generation ◽  
General Mechanism ◽  
Fusion Pore ◽  
Secretory Vesicles ◽  
Actin Assembly ◽  
Vesicle Membrane ◽  
Regulated Exocytosis ◽  
Broad Variety

Regulated exocytosis is thought to occur either by “full fusion,” where the secretory vesicle fuses with the plasma membrane (PM) via a fusion pore that then dilates until the secretory vesicle collapses into the PM; or by “kiss-and-run,” where the fusion pore does not dilate and instead rapidly reseals such that the secretory vesicle is retrieved almost fully intact. Here, we describe growing evidence for a third form of exocytosis, dubbed “kiss-and-coat,” which is characteristic of a broad variety of cell types that undergo regulated exocytosis. Kiss-and-coat exocytosis entails prolonged maintenance of a dilated fusion pore and assembly of actin filament (F-actin) coats around the exocytosing secretory vesicles followed by direct retrieval of some fraction of the emptied vesicle membrane. We propose that assembly of the actin coats results from the union of the secretory vesicle membrane and PM and that this compartment mixing represents a general mechanism for generating local signals via directed membrane fusion.

scholarly journals Processing of prothyrotropin-releasing hormone (Pro-TRH) by bovine intermediate lobe secretory vesicle membrane PC1 and PC2 enzymes.

Endocrinology ◽  
1995 ◽  
Vol 136 (10) ◽  
pp. 4462-4472 ◽  
Author(s):  
T C Friedman ◽  
Y P Loh ◽  
N X Cawley ◽  
N P Birch ◽  
S S Huang ◽  
...  
Keyword(s):  
Secretory Vesicle ◽  
Intermediate Lobe ◽  
Vesicle Membrane ◽  
Releasing Hormone

scholarly journals A19F-NMR study of the membrane-binding region of D-lactate dehydrogenase ofescherichia coli

1993 ◽  
Vol 2 (11) ◽  
pp. 1938-1947 ◽  
Author(s):  
Zhen-Yu Sun ◽  
Hoai-Thu N. Truong ◽  
E. A. Pratt ◽  
David C. Sutherland ◽  
Christine E. Kulig ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Membrane Binding ◽  
Ofescherichia Coli ◽  
Binding Region ◽  
Nmr Study

scholarly journals Complexin-2 redistributes to the membrane of muscle cells in response to insulin and contributes to GLUT4 translocation

2021 ◽  
Author(s):  
Martin Alejandro Pavarotti ◽  
Victoria Tokarz ◽  
Scott Frendo-Cumbo ◽  
Philip Bilan ◽  
Zhi Liu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Insulin Signalling ◽  
Muscle Cells ◽  
Secretory Vesicle ◽  
Vesicle Fusion ◽  
Glut4 Translocation ◽  
Vesicle Membrane ◽  
Actin Fiber ◽  
Complexin 2 ◽  
Intracellular Compartments

Insulin stimulates glucose uptake in muscle cells by rapidly redistributing vesicles containing GLUT4 glucose transporters from intracellular compartments to the plasma membrane. GLUT4 vesicle fusion requires formation of SNARE complexes between vesicular VAMP and plasma membrane syntaxin4 and SNAP23. SNARE accessory proteins usually regulate vesicle fusion processes. Complexins aide in neuro-secretory vesicle-membrane fusion by stabilizing trans-SNARE complexes but their participation in GLUT4 vesicle fusion is unknown. We report that complexin-2 is expressed and homogeneously distributed in L6 rat skeletal muscle cells. Upon insulin stimulation, a cohort of complexin-2 redistributes to the plasma membrane. Complexin-2 knockdown markedly inhibited GLUT4 translocation without affecting proximal insulin signalling of Akt/PKB phosphorylation and actin fiber remodelling. Similarly, complexin-2 overexpression decreased maximal GLUT4 translocation suggesting that the concentration of complexin-2 is finely tuned to vesicle fusion.  These findings reveal an insulin-dependent regulation of GLUT4 insertion into the plasma membrane involving complexin-2.

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