Dataset Information

Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product.

ABSTRACT: A cDNA for fascin, an actin-bundling protein in echinoderms, has been cloned, sequenced, and expressed. The predicted mass of the protein is approximately 55 kDa, similar to that observed for fascin purified from sea urchin eggs. Bacterially expressed fascin reacts with antibodies prepared against sea urchin egg fascin. Fascin has a strong sequence similarity to the singed gene (sn) product in Drosophila and has similarities with a 55-kDa human actin-bundling protein. No extensive similarities were found with other known actin-binding/bundling proteins, indicating that this is a separate gene family.

SUBMITTER: Bryan J

PROVIDER: S-EPMC47512 | biostudies-other | 1993 Oct

REPOSITORIES: biostudies-other

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Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product.

Bryan J J Edwards R R Matsudaira P P Otto J J Wulfkuhle J J

Proceedings of the National Academy of Sciences of the United States of America 19931001 19

A cDNA for fascin, an actin-bundling protein in echinoderms, has been cloned, sequenced, and expressed. The predicted mass of the protein is approximately 55 kDa, similar to that observed for fascin purified from sea urchin eggs. Bacterially expressed fascin reacts with antibodies prepared against sea urchin egg fascin. Fascin has a strong sequence similarity to the singed gene (sn) product in Drosophila and has similarities with a 55-kDa human actin-bundling protein. No extensive similarities w ...[more]

PMID: 8415664

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Project description:The assembly of actin-based structures with precisely defined architectures supports essential cellular functions, including motility, intracellular transport, and division. The geometric arrangements of the filaments within actin structures are stabilized via the association of crosslinking proteins, which bind two filaments simultaneously. Because actin polymerization and crosslinking occur concurrently within the dynamic environment of the cell, these processes likely play interdependent roles in shaping the architectures of actin-based structures. To dissect the contribution of polymerization to the construction of higher-order actin structures, we investigated how filament elongation affects the formation of simple, polarized actin bundles by the crosslinking protein fascin. Using populations of actin filaments to represent distinct stages of elongation, we found that the rate of bundle assembly increases with filament length. Fascin assembles short filaments into discrete bundles, whereas bundles of long filaments merge with one another to form interconnected networks. Although filament elongation promotes bundle coalescence, many connections formed between elongating bundles are short-lived and are followed by filament breakage. Our data suggest that initiation of crosslinking early in elongation aligns growing filaments, creating a template for continued bundle assembly as elongation proceeds. This initial alignment promotes the assembly of bundles that are resistant to large changes in curvature that are required for coalescence into interconnected networks. As a result, bundles of short filaments remain straighter and more topologically discrete as elongation proceeds than bundles assembled from long filaments. Thus, uncoordinated filament elongation and crosslinking can alter the architecture of bundled actin networks, highlighting the importance of maintaining precise control over filament length during the assembly of specialized actin structures.

Dataset Information

Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product.

Publications

Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product.

Similar Datasets

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