Dimensions of tubular invaginations of the plasma membrane associated with actin patches

Range diameter 50nm: length ≤180nm nm
Organism Budding yeast Saccharomyces cerevisiae
Reference Sirotkin V, Berro J, Macmillan K, Zhao L, Pollard TD. Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast. Mol Biol Cell. 2010 Aug 15 21(16):2894-904. doi: 10.1091/mbc.E10-02-0157. p.2894 left columnPubMed ID20587778
Primary Source Mulholland, J., Preuss, D., Moon, A., Wong, A., Drubin, D., and Botstein, D. (1994). Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J. Cell Biol. 125, 381–391. & Idrissi, F. Z., Grotsch, H., Fernandez-Golbano, I. M., Presciatto-Baschong, C., Riezman, H., and Geli, M. I. (2008). Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane. J. Cell Biol. 180, 1219–1232.PubMed ID8163554, 18347067
Comments "Clathrin-dependent endocytosis in yeast cells depends on the assembly of structures called actin patches (Kaksonen et al., 2006 Galletta and Cooper, 2009), which are associated with tubular invaginations of the plasma membrane 50 nm in diameter and up to 180 nm long in budding yeast (primary sources). The protein composition of actin patches evolves along a precisely timed pathway (Kaksonen et al., 2003, 2005 Sirotkin et al., 2005), beginning with recruitment of clathrin and endocytic adaptor proteins at the tip of a shallow invagination of the plasma membrane, followed by recruitment of activators of Arp2/3 complex to the base and side of the invagination (Kaksonen et al., 2003, 2005 Newpher et al., 2005 Idrissi et al., 2008)."
Entered by Uri M
ID 111106