Existence of a novel clathrin-independent endocytic pathway in yeast that depends on Rho1 and formin

J Cell Biol. 2011 Nov 14;195(4):657-71. doi: 10.1083/jcb.201104045. Epub 2011 Nov 7.

Abstract

Yeast is a powerful model organism for dissecting the temporal stages and choreography of the complex protein machinery during endocytosis. The only known mechanism for endocytosis in yeast is clathrin-mediated endocytosis, even though clathrin-independent endocytic pathways have been described in other eukaryotes. Here, we provide evidence for a clathrin-independent endocytic pathway in yeast. In cells lacking the clathrin-binding adaptor proteins Ent1, Ent2, Yap1801, and Yap1802, we identify a second endocytic pathway that depends on the GTPase Rho1, the downstream formin Bni1, and the Bni1 cofactors Bud6 and Spa2. This second pathway does not require components of the better-studied endocytic pathway, including clathrin and Arp2/3 complex activators. Thus, our results reveal the existence of a second pathway for endocytosis in yeast, which suggests similarities with the RhoA-dependent endocytic pathways of mammalian cells.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Clathrin / metabolism*
  • Endocytosis*
  • Microfilament Proteins / metabolism*
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • rho GTP-Binding Proteins / metabolism*

Substances

  • Bni1 protein, S cerevisiae
  • Clathrin
  • Microfilament Proteins
  • Saccharomyces cerevisiae Proteins
  • RHO1 protein, S cerevisiae
  • rho GTP-Binding Proteins