@article{TEXTUAL,
      recid = {10910},
      author = {Tsai, Feng-Ching and Henderson, J. Michael and Jarin, Zack  and Kremneva, Elena and Senju, Yosuke and Pernier, Julien  and Mikhajlov, Oleg and Manzi, John and Kogan, Konstantin  and Le Clainche, Christophe and Voth, Gregory A. and  Lappalainen, Pekka and Bassereau, Patricia},
      title = {Activated I-BAR IRSp53 clustering controls the formation  of VASP-actin–based membrane protrusions},
      journal = {Science Advances},
      address = {2022-10-14},
      number = {TEXTUAL},
      abstract = {Filopodia are actin-rich membrane protrusions essential  for cell morphogenesis, motility, and cancer invasion. How  cells control filopodium initiation on the plasma membrane  remains elusive. We performed experiments in cellulo, in  vitro, and in silico to unravel the mechanism of filopodium  initiation driven by the membrane curvature sensor IRSp53  (insulin receptor substrate protein of 53 kDa). We showed  that full-length IRSp53 self-assembles into clusters on  membranes depending on PIP2. Using well-controlled in vitro  reconstitution systems, we demonstrated that IRSp53  clusters recruit the actin polymerase VASP  (vasodilator-stimulated phosphoprotein) to assemble actin  filaments locally on membranes, leading to the generation  of actin-filled membrane protrusions reminiscent of  filopodia. By pulling membrane nanotubes from live cells,  we observed that IRSp53 can only be enriched and trigger  actin assembly in nanotubes at highly dynamic membrane  regions. Our work supports a regulation mechanism of IRSp53  in its attributes of curvature sensation and partner  recruitment to ensure a precise spatial-temporal control of  filopodium initiation.},
      url = {http://knowledge.uchicago.edu/record/10910},
}