The F-BAR Protein Syp1 Negatively Regulates WASp-Arp2/3 Complex Activity during Endocytic Patch Formation
- 3 December 2009
- journal article
- research article
- Published by Elsevier in Current Biology
- Vol. 19 (23) , 1979-1987
- https://doi.org/10.1016/j.cub.2009.10.062
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (F32-GM084677, R01-GM055796, R01-GM060979, R01-GM063691, R01-GM083137, T32-GM07231)
This publication has 62 references indexed in Scilit:
- Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulationThe EMBO Journal, 2009
- Protein structure prediction on the Web: a case study using the Phyre serverNature Protocols, 2009
- Actin and endocytosis: mechanisms and phylogenyCurrent Opinion in Cell Biology, 2009
- EFC/F-BAR proteins and the N-WASP–WIP complex induce membrane curvature-dependent actin polymerizationThe EMBO Journal, 2008
- Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membraneThe Journal of cell biology, 2008
- Spatial dynamics of receptor-mediated endocytic trafficking in budding yeast revealed by using fluorescent α-factor derivativesProceedings of the National Academy of Sciences, 2006
- Global landscape of protein complexes in the yeast Saccharomyces cerevisiaeNature, 2006
- Proteome survey reveals modularity of the yeast cell machineryNature, 2006
- A Pathway for Association of Receptors, Adaptors, and Actin during Endocytic InternalizationCell, 2003
- Molecular Architecture and Functional Model of the Endocytic AP2 ComplexCell, 2002