Plastins: versatile modulators of actin organization in (patho)physiological cellular processes

被引:135
作者
Delanote, V [1 ]
Vandekerckhove, J [1 ]
Gettemans, J [1 ]
机构
[1] State Univ Ghent VIB, Fac Med & Hlth Sci, Dept Med Prot Res, B-9000 Ghent, Belgium
关键词
actin; actin-binding protein; plastin; fimbrin; cytoskeleton;
D O I
10.1111/j.1745-7254.2005.00145.x
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Many actin-binding proteins are expressed in eukaryotic cells. These polypeptides assist in stabilizing and rearranging the organization of the actin cytoskeleton in response to external stimuli, or during cell migration and adhesion. Here we review a particular set of actin-binding proteins called plastins. Plastins (also called fimbrins) belong to a subclass of actin-binding proteins known as actin bundling, proteins. Three isoforms have been characterized in mammals: T-plastin is expressed in cells from solid tissue, whereas L-plastin occurs predominantly in hematopoietic cells. The third isoform, I-plastin, is specifically expressed in the small intestine, colon and kidney. These proteins share the unique property of cross-linking actin filaments into tight bundles. Although plastins are primarily involved in regulation of the actin cytoskeleton, they possess some unique features. For instance, they are implicated in invasion by pathogenic bacteria such as Shigella flexneri and Salmonella typhimurium. Also, L-plastin plays an important role in leukocyte function. T-plastin, on the other hand, is possibly involved in DNA repair. Finally, both T- and L-plastin are implicated in several diseases, and L-plastin is considered to be a valuable marker for cancer.
引用
收藏
页码:769 / 779
页数:11
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