| Literature DB >> 20585502 |
Sohail Ahmed, Wenyu Bu, Raphael Tze Chuen Lee, Sebastian Maurer-Stroh, Wah Ing Goh.
Abstract
The F-BAR domain is emerging as an important player in membrane remodeling pathways. F-BAR domain proteins couple membrane remodeling with actin dynamics associated with endocytic pathways and filopodium formation. Here, we provide a comprehensive analysis of F-BAR domain proteins in terms of their evolutionary relationships and protein function. F-BAR domain containing proteins can be categorized into five subfamilies based on their phylogeny which is consistent with the additional protein domains they possess, for example, RhoGAP domains, Cdc42 binding sites, SH3 domains and tyrosine kinase domains. We derive a protein-protein interaction network suggesting that dynamin1/2, N-WASP, Huntingtin, intersectin and Cdc42 are central nodes influencing F-BAR domain protein function.Entities:
Keywords: F-BAR; endocytosis; filopodium formation; membrane trafficking; morphology
Year: 2010 PMID: 20585502 PMCID: PMC2889966 DOI: 10.4161/cib.3.2.10808
Source DB: PubMed Journal: Commun Integr Biol ISSN: 1942-0889