This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3dad

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 22:06, 24 December 2014

Crystal structure of the N-terminal regulatory domains of the formin FHOD1

Structural highlights

3dad is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	FHOD1, FHOS, FHOS1 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[FHOD1_HUMAN] Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Formins induce the nucleation and polymerization of unbranched actin filaments. They share three homology domains required for profilin binding, actin polymerization, and regulation. Diaphanous-related formins (DRFs) are activated by GTPases of the Rho/Rac family, whose interaction with the N-terminal formin domain is thought to displace a C-terminal Diaphanous-autoregulatory domain (DAD). We have determined the structure of the N-terminal domains of FHOD1 consisting of a GTPase-binding domain (GBD) and the DAD-recognition domain FH3. In contrast to the formin mDia1, the FHOD1-GBD reveals a ubiquitin superfold as found similarly in c-Raf1 or PI3 kinase. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodeling. The FHOD1-FH3 domain is composed of five armadillo repeats, similarly to other formins. Mutation of one residue in the predicted DAD-interaction surface efficiently activates FHOD1 in cells. These results demonstrate that DRFs have evolved different molecular solutions to govern their autoregulation and GTPase specificity.

The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation.,Schulte A, Stolp B, Schonichen A, Pylypenko O, Rak A, Fackler OT, Geyer M Structure. 2008 Sep 10;16(9):1313-23. PMID:18786395^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Takeya R, Sumimoto H. Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation. J Cell Sci. 2003 Nov 15;116(Pt 22):4567-75. PMID:14576350 doi:http://dx.doi.org/10.1242/jcs.00769
↑ Gasteier JE, Schroeder S, Muranyi W, Madrid R, Benichou S, Fackler OT. FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation. Exp Cell Res. 2005 May 15;306(1):192-202. PMID:15878344 doi:http://dx.doi.org/S0014-4827(05)00052-2
↑ Hannemann S, Madrid R, Stastna J, Kitzing T, Gasteier J, Schonichen A, Bouchet J, Jimenez A, Geyer M, Grosse R, Benichou S, Fackler OT. The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing. J Biol Chem. 2008 Oct 10;283(41):27891-903. doi: 10.1074/jbc.M801800200. Epub, 2008 Aug 11. PMID:18694941 doi:10.1074/jbc.M801800200
↑ Schulte A, Stolp B, Schonichen A, Pylypenko O, Rak A, Fackler OT, Geyer M. The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation. Structure. 2008 Sep 10;16(9):1313-23. PMID:18786395 doi:10.1016/j.str.2008.06.008

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dad"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dad OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dad RCSB], [http://www.ebi.ac.uk/pdbsum/3dad PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/FHOD1_HUMAN FHOD1_HUMAN]] Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing.<ref>PMID:14576350</ref> <ref>PMID:15878344</ref> <ref>PMID:18694941</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3dad

From Proteopedia

Revision as of 22:06, 24 December 2014

Crystal structure of the N-terminal regulatory domains of the formin FHOD1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox