Coordinated Actions of Actin and BAR Proteins Upstream of Dynamin at Endocytic Clathrin-Coated Pits

Shawn Ferguson, Andrea Raimondi, Summer Paradise, Hongying Shen, Kumi Mesaki, Agnes Ferguson, Olivier Destaing, Genevieve Ko, Junko Takasaki, Ottavio Cremona, Eileen O' Toole, Pietro De Camilli

Research output: Contribution to journalArticlepeer-review


The GTPase dynamin, a key player in endocytic membrane fission, interacts with numerous proteins that regulate actin dynamics and generate/sense membrane curvature. To determine the functional relationship between these proteins and dynamin, we have analyzed endocytic intermediates that accumulate in cells that lack dynamin (derived from dynamin 1 and 2 double conditional knockout mice). In these cells, actin-nucleating proteins, actin, and BAR domain proteins accumulate at the base of arrested endocytic clathrin-coated pits, where they support the growth of dynamic long tubular necks. These results, which we show reflect the sequence of events in wild-type cells, demonstrate a concerted action of these proteins prior to, and independent of, dynamin and emphasize similarities between clathrin-mediated endocytosis in yeast and higher eukaryotes. Our data also demonstrate that the relationship between dynamin and actin is intimately connected to dynamin's endocytic role and that dynamin terminates a powerful actin- and BAR protein-dependent tubulating activity.

Original languageEnglish
Pages (from-to)811-822
Number of pages12
JournalDevelopmental Cell
Issue number6
Publication statusPublished - Dec 15 2009



ASJC Scopus subject areas

  • Developmental Biology


Dive into the research topics of 'Coordinated Actions of Actin and BAR Proteins Upstream of Dynamin at Endocytic Clathrin-Coated Pits'. Together they form a unique fingerprint.

Cite this