scholarly journals Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites

2003 ◽  
Vol 163 (3) ◽  
pp. 559-570 ◽  
Author(s):  
Claire Desnos ◽  
Jean-Sébastien Schonn ◽  
Sébastien Huet ◽  
Viet Samuel Tran ◽  
Aziz El-Amraoui ◽  
...  
Keyword(s):  
Pc12 Cells ◽  
Evanescent Wave ◽  
Chromaffin Cells ◽  
Secretory Granules ◽  
Adrenal Chromaffin Cells ◽  
Actin Cortex ◽  
Myosin Va ◽  
Myosin Viia ◽  
Adrenal Chromaffin ◽  
And Control

The GTPase Rab27A interacts with myosin-VIIa and myosin-Va via MyRIP or melanophilin and mediates melanosome binding to actin. Here we show that Rab27A and MyRIP are associated with secretory granules (SGs) in adrenal chromaffin cells and PC12 cells. Overexpression of Rab27A, GTPase-deficient Rab27A-Q78L, or MyRIP reduced secretory responses of PC12 cells. Amperometric recordings of single adrenal chromaffin cells revealed that Rab27A-Q78L and MyRIP reduced the sustained component of release. Moreover, these effects on secretion were partly suppressed by the actin-depolymerizing drug latrunculin but strengthened by jasplakinolide, which stabilizes the actin cortex. Finally, MyRIP and Rab27A-Q78L restricted the motion of SGs in the subplasmalemmal region of PC12 cells, as measured by evanescent-wave fluorescence microscopy. In contrast, the Rab27A-binding domain of MyRIP and a MyRIP construct that interacts with myosin-Va but not with actin increased the mobility of SGs. We propose that Rab27A and MyRIP link SGs to F-actin and control their motion toward release sites through the actin cortex.

PC12 Cells as a Model to Study the Effects of Opioids on Normal and Tumoral Adrenal Chromaffin Cells

1995 ◽  
Vol 771 (1 Stress) ◽  
pp. 166-172 ◽  
Author(s):  
A. N. MARGIORIS ◽  
M. VENIHAKI ◽  
C. STOURNARAS ◽  
A. GRAVANIS
Keyword(s):  
Pc12 Cells ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin

scholarly journals Exophilin-8 assembles secretory granules for exocytosis in the actin cortex via interaction with RIM-BP2 and myosin-VIIa

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Fushun Fan ◽  
Kohichi Matsunaga ◽  
Hao Wang ◽  
Ray Ishizaki ◽  
Eri Kobayashi ◽  
...  
Keyword(s):  
Secretory Granules ◽  
Direct Interaction ◽  
Null Mouse ◽  
Cell Periphery ◽  
Actin Network ◽  
Actin Cortex ◽  
Granule Membrane ◽  
Mouse Pancreatic Islets ◽  
Myosin Va ◽  
Myosin Viia

Exophilin-8 has been reported to play a role in anchoring secretory granules within the actin cortex, due to its direct binding activities to Rab27 on the granule membrane and to F-actin and its motor protein, myosin-Va. Here, we show that exophilin-8 accumulates granules in the cortical F-actin network not by direct interaction with myosin-Va, but by indirect interaction with a specific form of myosin-VIIa through its previously unknown binding partner, RIM-BP2. RIM-BP2 also associates with exocytic machinery, Cav1.3, RIM, and Munc13-1. Disruption of the exophilin-8–RIM-BP2–myosin-VIIa complex by ablation or knockdown of each component markedly decreases both the peripheral accumulation and exocytosis of granules. Furthermore, exophilin-8-null mouse pancreatic islets lose polarized granule localization at the β-cell periphery and exhibit impaired insulin secretion. This newly identified complex acts as a physical and functional scaffold and provides a mechanism supporting a releasable pool of granules within the F-actin network beneath the plasma membrane.

scholarly journals Presence of Dynamin-Syntaxin Complexes Associated with Secretory Granules in Adrenal Chromaffin Cells

2002 ◽  
Vol 75 (4) ◽  
pp. 1511-1519 ◽  
Author(s):  
Marie-Christine Galas ◽  
Sylvette Chasserot-Golaz ◽  
Sylvie Dirrig-Grosch ◽  
Marie-France Bader
Keyword(s):  
Chromaffin Cells ◽  
Secretory Granules ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin

scholarly journals A Cysteine-rich Domain Defined by a Novel Exon in aSloVariant in Rat Adrenal Chromaffin Cells and PC12 Cells

1997 ◽  
Vol 272 (18) ◽  
pp. 11710-11717 ◽  
Author(s):  
Mitsuyoshi Saito ◽  
Carl Nelson ◽  
Lawrence Salkoff ◽  
Christopher J. Lingle
Keyword(s):  
Pc12 Cells ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Rich Domain ◽  
Adrenal Chromaffin ◽  
Novel Exon ◽  
Cysteine Rich Domain

Morphological Observations on the Granule Types in Rabbit Extra-Adrenal Chromaffin Cells.

1975 ◽  
Vol 33 ◽  
pp. 318-319
Author(s):  
Joe A. Mascorro ◽  
Robert D. Yates
Keyword(s):  
Chromaffin Cells ◽  
Sodium Phosphate ◽  
Ganglion Cells ◽  
Ultrastructural Level ◽  
Osmic Acid ◽  
Adrenal Chromaffin Cells ◽  
Potassium Iodate ◽  
Perfusion Fluid ◽  
New Zealand White Rabbits ◽  
Adrenal Chromaffin

Extra-adrenal chromaffin organs (abdominal paraganglia) constitute rich sources of catecholamines. It is believed that these bodies contain norepinephrine exclusively. However, the present workers recently observed epinephrine type granules in para- ganglion cells. This report investigates catecholamine containing granules in rabbit paraganglia at the ultrastructural level.New Zealand white rabbits (150-170 grams) were anesthetized with 50 mg/kg Nembutal (IP) and perfused with 3% glutaraldehyde buffered with 0.2M sodium phosphate, pH 7.3. The retroperitoneal tissue blocks were removed and placed in perfusion fluid for 4 hours. The abdominal paraganglia were dissected from the blocks, diced, washed in phosphate buffer and fixed in 1% osmic acid buffered with phosphate. In other animals, the glutaraldehyde perfused tissue blocks were immersed for 1 hour in 3% glutaraldehyde/2.5% potassium iodate buffered as before. The paraganglia were then diced, separated into two vials and washed in the buffer. A portion of this tissue received osmic acid fixation.

scholarly journals Stimulatory effect of serotonin on Na+-dependent Ca2+ efflux from bovine adrenal chromaffin cells in culture

1997 ◽  
Vol 73 ◽  
pp. 226
Author(s):  
Kazuo Minakuchi ◽  
Hitoshi Houchi ◽  
Masanori Yoshizumi ◽  
Yasuko Ishimura ◽  
Kyoji Morita ◽  
...  
Keyword(s):  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Cells In Culture ◽  
Adrenal Chromaffin
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