The actin binding protein scinderin acts in PC12 cells to tether dense-core vesicles prior to secretion.
Mol Cell Neurosci
; 85: 12-18, 2017 12.
Article
em En
| MEDLINE
| ID: mdl-28823945
ABSTRACT
Mechanistic understanding of the control of vesicle motion from within a secretory cell to the site of exocytosis remains incomplete. In this work, we have used total internal reflection (TIRF) microscopy to examine the mobility of secretory vesicles at the plasma membrane. Under resting conditions, we found vesicles showed little lateral mobility. Anchoring of vesicles in this membrane proximal compartment could be disrupted with latrunculin A, indicating an apparent actin dependent process. A candidate intermediary between vesicles and the actin skeleton is the actin binding protein scinderin. Co-transfection of an shRNA construct against scinderin blocked secretion, and also increased the mobility of vesicles in the membrane-proximal section of the cell, indicating a dual role for scinderin in secretion; tethering vesicles to the cytoskeleton, as well as liberating them following stimulation through the previously described calcium dependent actin severing activity. Analysis of lipid dependence indicates that scinderin exhibits calcium dependent binding to phosphatidyl-inositol monophosphate, providing a possible mechanism for vesicle binding.
Palavras-chave
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Gelsolina
/
Vesículas Secretórias
/
Exocitose
Limite:
Animals
Idioma:
En
Revista:
Mol Cell Neurosci
Assunto da revista:
BIOLOGIA MOLECULAR
/
NEUROLOGIA
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
Estados Unidos