Eisosomes mark static sites of endocytosis.
Endocytosis functions to recycle plasma membrane components, to regulate cell-surface expression of signalling receptors and to internalize nutrients in all eukaryotic cells. Internalization of proteins, lipids and other cargo can occur by one of several pathways that have different, but often overlapping, molecular requirements. To mediate endocytosis, effectors assemble transiently underneath the plasma membrane, carry out the mechanics of membrane deformation, cargo selection and vesicle internalization, and then disassemble. The mechanism by which endocytosis initiates at particular locations on the plasma membrane has remained unknown. Sites of endocytosis might be formed randomly, induced by stochastic protein and/or lipid clustering. Alternatively, endocytosis might initiate at specific locations. Here we describe large immobile protein assemblies at the plasma membrane in the yeast Saccharomyces cerevisiae that mark endocytic sites. These structures, termed eisosomes (from the Greek 'eis', meaning into or portal, and 'soma', meaning body), are composed primarily of two cytoplasmic proteins, Pil1 and Lsp1. A plasma membrane protein, Sur7, localizes to eisosomes. These structures colocalize with sites of protein and lipid endocytosis, and their components genetically interact with known endocytic effectors. Loss of Pil1 leads to clustering of eisosome remnants and redirects endocytosis and endocytic effector proteins to these clusters.
Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California at San Francisco, 600-16th Street, San Francisco, California 94143-2200, USA. twalther@itsa.ucsf.edu
Tobias C
TC
Walther
Jason H
JH
Brickner
Pablo S
PS
Aguilar
Sebastián
S
Bernales
Carlos
C
Pantoja
Peter
P
Walter
D000199:Actins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism*; D004705:Endocytosis; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology* / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*
D000199:Actins; C487328:LSP1 protein, S cerevisiae; D008565:Membrane Proteins; D046912:Multiprotein Complexes; C487327:PIL1 protein, S cerevisiae; D010750:Phosphoproteins; C502213:SUR7 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins