BIOLOGICAL BASKET WEAVING: Formation and Function of Clathrin-Coated Vesicles

• Published in: Annual review of cell and developmental biology Vol. 17; no. 1; pp. 517 - 568
• Main Authors: Brodsky, Frances M, Chen, Chih-Ying, Knuehl, Christine, Towler, Mhairi C, Wakeham, Diane E
• Format: Journal Article
• Language: English
• Published: Palo Alto, CA 94303-0139 Annual Reviews 01.01.2001; 4139 El Camino Way, P.O. Box 10139 Annual Reviews, Inc; USA
• Subjects: adaptor; Adaptor Proteins, Vesicular Transport; Animals; Carrier Proteins - metabolism; Cell Polarity - physiology; Clathrin - chemistry; Clathrin - metabolism; Clathrin-Coated Vesicles - metabolism; Clathrin-Coated Vesicles - physiology; Coated Pits, Cell-Membrane - metabolism; cytoskeleton; Cytoskeleton - metabolism; endocytosis; Endocytosis - physiology; Humans; Membrane Proteins - metabolism; Models, Molecular; Muscle, Skeletal - metabolism; Neurons - metabolism; Protein Transport - physiology; secretion; sorting
• ISSN: 1081-0706; 1530-8995
• DOI: 10.1146/annurev.cellbio.17.1.517

There has recently been considerable progress in understanding the regulation of clathrin-coated vesicle (CCV) formation and function. These advances are due to the determination of the structure of a number of CCV coat components at molecular resolution and the identification of novel regulatory proteins that control CCV formation in the cell. In addition, pathways of ( a ) phosphorylation, ( b ) receptor signaling, and ( c ) lipid modification that influence CCV formation, as well as the interaction between the cytoskeleton and CCV transport pathways are becoming better defined. It is evident that although clathrin coat assembly drives CCV formation, this fundamental reaction is modified by different regulatory proteins, depending on where CCVs are forming in the cell. This regulatory difference likely reflects the distinct biological roles of CCVs at the plasma membrane and trans -Golgi network, as well as the distinct properties of these membranes themselves. Tissue-specific functions of CCVs require even more-specialized regulation and defects in these pathways can now be correlated with human diseases.