Actin assembly and endocytosis: from yeast to mammals

Annu Rev Cell Dev Biol. 2003;19:287-332. doi: 10.1146/annurev.cellbio.19.111401.093127.


Internalization of receptors, lipids, pathogens, and other cargo at the plasma membrane involves several different pathways and requires coordinated interactions between a variety of protein and lipid molecules. The actin cytoskeleton is an integral part of the cell cortex, and there is growing evidence that F-actin plays a direct role in these endocytic events. Genetic studies in yeast have firmly established a functional connection between actin and endocytosis. Identification of several proteins that may function at the interface between actin and the endocytic machinery has provided further evidence for this association in both yeast and mammalian cells. Several of these proteins are directly involved in regulating actin assembly and could thus harness forces produced during actin polymerization to facilitate specific steps in the endocytic process. Recent microscopy studies in mammalian cells provide powerful evidence that localized recruitment and polymerization of actin occurs at endocytic sites. In this review, we focus on progress made in elucidating the functions of the actin cytoskeleton in endocytosis.

Publication types

  • Review

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Actin-Related Protein 2
  • Actins / metabolism*
  • Animals
  • Caveolae / metabolism
  • Cell Membrane Structures / metabolism*
  • Clathrin / metabolism
  • Dynamins / metabolism
  • Endocytosis / physiology*
  • Humans
  • Saccharomyces cerevisiae Proteins / metabolism
  • Yeasts / metabolism


  • ARP2 protein, S cerevisiae
  • Actin-Related Protein 2
  • Actins
  • Clathrin
  • Saccharomyces cerevisiae Proteins
  • Dynamins