The Actin-Bundling Protein L-Plastin: A Critical Regulator of Immune Cell Function
Author(s) -
Sharon Celeste Morley
Publication year - 2011
Publication title -
international journal of cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.587
H-Index - 53
eISSN - 1687-8884
pISSN - 1687-8876
DOI - 10.1155/2012/935173
Subject(s) - podosome , lamellipodium , microbiology and biotechnology , actin , immune system , cytoplasm , biology , actin cytoskeleton , motility , cytoskeleton , chemistry , cell , immunology , biochemistry
L-plastin is a leukocyte-specific protein that cross-links actin filaments into tight bundles, increasing the stability of actin-based structures such as podosomes and lamellipodia. While first identified as an abundant cytoplasmic protein in hematopoietically derived cells over 25 years ago, the requirement for L-plastin in multiple functions critical for immunity, such as antigen receptor signaling, adhesion, and motility, has only recently become clear. L-plastin has been identified as an important component in cellular processes critical for neutrophil, macrophage, osteoclast, eosinophil, and T- and B-lymphocyte biology. Following a brief description of the structure and function of L-plastin, the regulation of immune cell functions by L-plastin will be reviewed in detail.
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