Human Platelets Contain Scinderin, a Ca2+-Dependent Actin Filament-Severing Protein

A, Rodríguez Del Castillo; Ml, Vitale; Tchakarov, L.; Jm, Trifaró

doi:10.1055/s-0038-1648420

Cited by 30 publications

(12 citation statements)

References 13 publications

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“…The N-terminus of scinderin binds actin and PIP2 and both interactions are required during agonist stimulation in chromaffin cells [217, 218]. Although scinderin plays a role in other secretory events, such as mucin secretion in airway cells [219] or insulin secretion in β-cells [220], its expression is limited to few tissues [221] suggesting the involvement of other actin severing proteins.…”

Section: Role Of the Actin Cytoskeleton In Pre-fusion Stepsmentioning

confidence: 99%

Multiple roles for the actin cytoskeleton during regulated exocytosis

Porat-Shliom

Milberg

Masedunskas

et al. 2012

Cell. Mol. Life Sci.

167

162

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Regulated exocytosis is the main mechanism utilized by specialized secretory cells to deliver molecules to the cell surface by virtue of membranous containers (i.e. secretory vesicles). The process involves a series of highly coordinated and sequential steps, which include the biogenesis of the vesicles, their delivery to the cell periphery, their fusion with the plasma membrane and the release of their content into the extracellular space. Each of these steps is regulated by the actin cytoskeleton. In this review, we summarize the current knowledge regarding the involvement of actin and its associated molecules during each of the exocytic steps in vertebrates, and suggest that the overall role of the actin cytoskeleton during regulated exocytosis is linked to the architecture and the physiology of the secretory cells under examination. Specifically, in neurons, neuroendocrine, endocrine, and hematopoietic cells, which contain small secretory vesicles that undergo rapid exocytosis (on the order of milliseconds), the actin cytoskeleton plays a role in pre-fusion events, where it acts primarily as a functional barrier and facilitates docking. In exocrine and other secretory cells, which contain large secretory vesicles that undergo slow exocytosis (seconds to minutes), the actin cytoskeleton plays a role in post-fusion events, where it regulates the dynamics of the fusion pore, facilitates the integration of the vesicles into the plasma membrane, provides structural support, and promotes the expulsion of large cargo molecules.

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Section: Role Of the Actin Cytoskeleton In Pre-fusion Stepsmentioning

confidence: 99%

Multiple roles for the actin cytoskeleton during regulated exocytosis

Porat-Shliom

Milberg

Masedunskas

et al. 2012

Cell. Mol. Life Sci.

167

162

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“…As compared to gelsolin, adseverin has a more restricted expression. Adseverin was first discovered in platelets, megakaryocytes and chromaffin cells [19]. This protein is present in all secretory cells and is involved in actin cytoskeleton remodeling occurring during exocytosis [19 -22].…”

Section: Review Articlementioning

confidence: 99%

Gelsolin superfamily proteins: key regulators of cellular functions

Silacci

Mazzolai²,

Gauci

et al. 2004

CMLS, Cell. Mol. Life Sci.

368

317

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Cytoskeletal rearrangement occurs in a variety of cellular processes and involves a wide spectrum of proteins. Among these, the gelsolin superfamily proteins control actin organization by severing filaments, capping filament ends and nucleating actin assembly [1]. Gelsolin is the founding member of this family, which now contains at least another six members: villin, adseverin, capG, advillin, supervillin and flightless I. In addition to their respective role in actin filament remodeling, these proteins have some specific and apparently non-overlapping particular roles in several cellular processes, including cell motility, control of apoptosis and regulation of phagocytosis (summarized in table 1). Evidence suggests that proteins belonging to the gelsolin superfamily may be involved in other processes, including gene expression regulation. This review will focus on some of the known functions of the gelsolin superfamily proteins, thus providing a basis for reflection on other possible and as yet incompletely understood roles for these proteins.

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“…Among the last category, gelsolin and scinderin are 2 Ca ϩϩ -dependent, filamentous actin-severing proteins found in normal megakaryocytes and platelets. 12,13 Scinderin was discovered in chromaffin cells, and its gene was cloned in our laboratory. [14][15][16] This protein, which is present in all secretory cells, 17 controls dynamic changes observed in cortical F-actin during secretion.…”

Section: Introductionmentioning

confidence: 99%