Synergistic BAR-NPF interactions in actin-driven membrane remodeling.
Cell and organelle shape can profoundly influence proper cellular function. In recent years, two machineries have emerged as major regulators of membrane shape: Bin-Amphiphysin-Rvs161/167 (BAR) domain-containing proteins, which induce membrane invaginations or protrusions, and nucleation promoting factors (NPFs), which activate the Arp2/3 complex and are thus responsible for the generation of branched actin networks that push on membranes. Several BAR-NPF interactions have been shown to induce various types of protrusions, such as lamellipodia or filopodia, or invaginations, including trafficking organelles such as caveolae, endosomes and clathrin-coated pits (CCPs). This review focuses on how collaboration between these two interacting machineries, which emerges as a unified mechanism of membrane remodeling, accounts for such a variety of membrane shapes.
Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1, Yayoi, Tokyo, 113-0032, Japan. suetsugu@iam.u-tokyo.ac.jp
Shiro
S
Suetsugu
Alexis
A
Gautreau
D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding
D000199:Actins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C075637:amphiphysin