Drf_GBDDiaphanous GTPase-binding Domain |
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| SMART accession number: | SM01140
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| Description: |
This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein. |
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| Family alignment: |
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There are 635
Drf_GBD domains in 635 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Peng J, Wallar BJ, Flanders A, Swiatek PJ, Alberts AS
- Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals arole for Drf3 as an effector for Cdc42.
- Curr Biol. 2003; 13: 534-45
- Display abstract
BACKGROUND: Mammalian Diaphanous-related formins (Drfs) act as Rho small GTPaseeffectors during growth factor-induced cytoskeletal remodeling and cell division.While both p140 mDia1 (herein called Drf1) and p134 mDia2 (Drf3) have been shown to bind in vitro to activated RhoA-C, and Drf3 has also been shown to bind toCdc42, little is known about the cellular function of these GTPase effectorpairs. Thus, we have begun targeting the murine Drf genes to address theirvarious contributions to small GTPase signaling in cytoskeletal remodeling anddevelopment. RESULTS: Drf1 +/+, +/-, and -/- cell lines were derived fromembryonic stem cells. While some Drf1 +/- lines had fewer actin stress fibers,several Drf1 +/- and -/- cells were more motile and had more abundant lamella andfilopodia. Because the apparent "gain-of-function" corresponded with elevatedlevels of Drf3 protein expression, we hypothesized that the effects on the actin cytoskeleton were due to Cdc42 utilization of Drf3 as an effector. In this study,we found that inactive Drf3 variants and microinjected Drf3 antibodies interferedwith Cdc42-induced filopodia. In addition, we observed that Drf3 contains apreviously unidentified CRIB-like motif within its GTPase binding domain (GBD).By fluorescent resonance energy transfer (FRET) analysis, we demonstrate thatthis motif is required for Cdc42 binding and Drf3 recruitment to the leading edgeand, surprisingly, to the microtubule organizing center (MTOC) of migratingfibroblasts. CONCLUSIONS: Our observations extend the role of the mammalian Drfs in cell signaling and demonstrate that Cdc42 not only activates Drf3, but guides the effector to sites at the cell cortex where it remodels the actincytoskeleton.
- Structure (3D structures containing this domain)
3D Structures of Drf_GBD domains in PDB
| PDB code | Main view | Title | | 1z2c |  | Crystal structure of mdia1 gbd-fh3 in complex with rhoc- gmppnp |
| 2bap |  | Crystal structure of the n-terminal mdia1 armadillo repeat region and dimerisation domain in complex with the mdia1 autoregulatory domain (dad) |
| 2bnx |  | Crystal structure of the dimeric regulatory domain of mouse diaphaneous-related formin (drf), mdia1 |
| 2f31 |  | Crystal structure of the autoinhibitory switch in formin mdia1; the did/dad complex |
| 3eg5 |  | Crystal structure of mdia1-tsh gbd-fh3 in complex with cdc42-gmppnp |
- Links (links to other resources describing this domain)
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