title: Reversible membrane pearling in live cells upon destruction of the actin cortex.
abstract: Membrane pearling in live cells is observed when the plasma membrane is depleted of its support, the cortical actin network. Upon efficient depolymerization of actin, pearls of variable size are formed, which are connected by nanotubes of ~40 nm diameter. We show that formation of the membrane tubes and their transition into chains of pearls do not require external tension, and that they neither depend on microtubule-based molecular motors nor pressure generated by myosin-II. Pearling thus differs from blebbing. The pearling state is stable as long as actin is prevented from polymerizing. When polymerization is restored, the pearls are retracted into the cell, indicating continuity of the membrane. Our data suggest that the alternation of pearls and strings is an energetically favored state of the unsupported plasma membrane, and that one of the functions of the actin cortex is to prevent the membrane from spontaneously assuming this configuration.
authors.affiliation: Leiden Institute of Physics, LION, Leiden University, The Netherlands; Fraunhofer-Institut für Silicatforschung ISC, Würzburg, Germany.
authors.forename: Doris
authors.initials: D
authors.lastname: Heinrich
authors.affiliation: Max Planck Institute of Biochemistry, Martinsried, Germany.
authors.forename: Mary
authors.initials: M
authors.lastname: Ecke
authors.affiliation: Max Planck Institute of Biochemistry, Martinsried, Germany.
authors.forename: Marion
authors.initials: M
authors.lastname: Jasnin
authors.affiliation: Nikon Imaging Center, Heidelberg, Germany.
authors.forename: Ulrike
authors.initials: U
authors.lastname: Engel
authors.affiliation: Max Planck Institute of Biochemistry, Martinsried, Germany. Electronic address: gerisch@biochem.mpg.de.
authors.forename: Günther
authors.initials: G
authors.lastname: Gerisch
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism / Q000648:ultrastructure; D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D001696:Biomechanical Phenomena; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D002470:Cell Survival; D020285:Cryoelectron Microscopy; D004023:Dictyostelium / Q000166:cytology; D005898:Glass / Q000737:chemistry; D008870:Microtubules / Q000378:metabolism; D024462:Myosin Type II / Q000378:metabolism; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D013499:Surface Properties
chemical_list: D000199:Actins; D024462:Myosin Type II