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Comment
. 2006 Mar 14;103(11):3953-4.
doi: 10.1073/pnas.0600658103. Epub 2006 Mar 7.

There's a GAP in the ENTH domain

Affiliations
Comment

There's a GAP in the ENTH domain

Brigitte Ritter et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

Conflict of interest statement: No conflicts declared.

Figures

Fig. 1.
Fig. 1.
Backbone trace of the ENTH domain of rat epsin crystallized in complex with inositol (1,4,5)P3 (red), which is used as a mimic of PtdIns(4,5)P2 (PIP2) head groups at the membrane. The structure is from PTB1H0A. α0 is shown to insert into the inner leaflet of the bilayer. Y100, T104, and E137, which form a surface patch for interactions with Cdc42 GAPs, are in pink.
Fig. 2.
Fig. 2.
Model of the potential roles of the ENTH domain of Ent1/2p. Clathrin and endocytic regulatory proteins (purple), including Ent1/2p (the ENTH domain alone is shown), localize to sites of endocytosis where they contribute to membrane deformation and curvature. By means of the actions of Arp2/3, actin (green) assembles into an actin patch that contributes to membrane invagination. The ENTH domains bind and sequester/inhibit Cdc42 GAPs, allowing for local activation of Cdc42. Through a Gic1/2/Bni1 pathway, actin cables are assembled that direct secretory vesicle in a myosin-dependent manner. Cdc42·GTP can also contribute to actin patch formation by signaling to activation of Arp2/3.

Comment on

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