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Perspectives

Linking up at the BAR: Oligomerization and F-BAR protein function

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Pages 1977-1985 | Received 13 Apr 2016, Accepted 11 May 2016, Published online: 23 Jun 2016

Figures & data

Figure 1. Human, S. pombe, and S. cerevisiae F-BAR proteins. Conserved domain layouts and select binding partners or substrates of human, S. pombe, and S. cerevisiae F-BAR proteins. Dashed lines indicate the domain is present only in a subset of the listed F-BAR proteins. *Indicates data from Drosophila homologs. Indicates data from mouse or rat homologs.

Figure 1. Human, S. pombe, and S. cerevisiae F-BAR proteins. Conserved domain layouts and select binding partners or substrates of human, S. pombe, and S. cerevisiae F-BAR proteins. Dashed lines indicate the domain is present only in a subset of the listed F-BAR proteins. *Indicates data from Drosophila homologs. †Indicates data from mouse or rat homologs.

Figure 2. Diverse modes of F-BAR oligomerization in endocytosis, cytokinesis, and cell migration. Schematics of possible modes of F-BAR protein oligomerization, protein recruitment, and signaling in endocytosis, cytokinesis, and cell migration.

Figure 2. Diverse modes of F-BAR oligomerization in endocytosis, cytokinesis, and cell migration. Schematics of possible modes of F-BAR protein oligomerization, protein recruitment, and signaling in endocytosis, cytokinesis, and cell migration.

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