Abstract
Clathrin is a cytosolic protein involved in the intracellular trafficking of a wide range of cargo. It is composed of three heavy chains and three light chains that together form a triskelion, the subunit that polymerizes to form a clathrin coated vesicle. In addition to its role in membrane trafficking, clathrin is also involved in various cellular and biological processes such as chromosomal segregation during mitosis and organelle biogenesis. Although the role of the heavy chains in regulating important physiological processes has been well documented, we still lack a complete understanding of how clathrin light chains regulate membrane traffic and cell signaling. This review highlights the importance and contributions of clathrin light chains in regulating clathrin assembly, vesicle formation, endocytosis of selective receptors and physiological and developmental processes.
Highlights
Endocytosis is a process carried out by eukaryotic cells to internalize extracellular molecules, plasma membrane proteins and lipids (Doherty and McMahon, 2009)
clathrin mediated endocytosis (CME) is characterized by the recruitment of clathrin and its associated molecules to the plasma membrane allowing the formation of clathrin-coated vesicles (CCVs)
A triskelion is composed of three clathrin heavy chains (CHC) (∼190 kDa) each of which is associated with a smaller clathrin light chain (CLC) (∼25 kDa)
Summary
Endocytosis is a process carried out by eukaryotic cells to internalize extracellular molecules, plasma membrane proteins and lipids (Doherty and McMahon, 2009). Vertebrate CLCs contain a consensus region of 22 amino acids shared by both CLCa and CLCb. they include distinct domains for binding to calcium, clathrin heavy chain, calmodulin and a neuron-specific insertion sequence (Brodsky, 2012). Despite having 60% sequence similarity, the two light chains are diverse in nature due to alternative splicing, internal disulfide bond formation and tissue specific expression patterns, allowing speculation that their ability to perform distinct physiological and functional roles could be attributed to such differences.
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