2gyt

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the SAM (sterile alpha motif) domain of DLC1 (deleted in liver cancer 1)

Structural highlights

2gyt is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RHG07_HUMAN Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality.^[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

Deleted in liver cancer 1 (DLC1) is a multi-modular Rho-GTPase-activating protein (RhoGAP) and a tumor suppressor. Besides its RhoGAP domain, functions of other domains in DLC1 remain largely unknown. By protein precipitation and mass spectrometry, we identified eukaryotic elongation factor 1A1 (EF1A1) as a novel partner for the sterile alpha motif (SAM) domain of DLC1 but not the SAM domain of DLC2. The solution structure of DLC1 SAM revealed a new monomeric fold with four parallel helices, similar to that of DLC2 SAM but distinct from other SAM domains. Mutating F38, L39 and F40 within a hydrophobic patch retained its overall structure but abolished its interaction with EF1A1 with F38 and L39 forming an indispensable interacting motif. DLC1 SAM did not localize to and was not required for DLC1 to suppress the turnover of focal adhesions. Instead, DLC1 SAM facilitated EF1A1 distribution to the membrane periphery and ruffles upon growth factor stimulation. Compared with wild-type DLC1, the non-interactive DLC1 mutant is less potent in suppressing cell migration, whereas overexpression of the DLC1 SAM domain alone, but not the non-interactive mutant SAM or DLC2 SAM, greatly enhanced cell migration. This finding reveals a novel contribution of the SAM-EF1A1 interaction as a potentially important GAP-independent modulation of cell migration by DLC1.

The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell migration.,Zhong D, Zhang J, Yang S, Soh UJ, Buschdorf JP, Zhou YT, Yang D, Low BC J Cell Sci. 2009 Feb 1;122(Pt 3):414-24. PMID:19158340^[4]

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

References

↑ Kim TY, Healy KD, Der CJ, Sciaky N, Bang YJ, Juliano RL. Effects of structure of Rho GTPase-activating protein DLC-1 on cell morphology and migration. J Biol Chem. 2008 Nov 21;283(47):32762-70. doi: 10.1074/jbc.M800617200. Epub 2008, Sep 11. PMID:18786931 doi:10.1074/jbc.M800617200
↑ Kawai K, Iwamae Y, Yamaga M, Kiyota M, Ishii H, Hirata H, Homma Y, Yagisawa H. Focal adhesion-localization of START-GAP1/DLC1 is essential for cell motility and morphology. Genes Cells. 2009 Feb;14(2):227-41. doi: 10.1111/j.1365-2443.2008.01265.x. Epub, 2008 Jan 15. PMID:19170769 doi:10.1111/j.1365-2443.2008.01265.x
↑ Erlmann P, Schmid S, Horenkamp FA, Geyer M, Pomorski TG, Olayioye MA. DLC1 activation requires lipid interaction through a polybasic region preceding the RhoGAP domain. Mol Biol Cell. 2009 Oct;20(20):4400-11. doi: 10.1091/mbc.E09-03-0247. Epub 2009, Aug 26. PMID:19710422 doi:10.1091/mbc.E09-03-0247
↑ Zhong D, Zhang J, Yang S, Soh UJ, Buschdorf JP, Zhou YT, Yang D, Low BC. The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell migration. J Cell Sci. 2009 Feb 1;122(Pt 3):414-24. PMID:19158340 doi:122/3/414

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/2gyt"

Categories: Homo sapiens | Large Structures | Yang S

@@ Line 1: / Line 1: @@
 ==Solution structure of the SAM (sterile alpha motif) domain of DLC1 (deleted in liver cancer 1)==
-<StructureSection load='2gyt' size='340' side='right' caption='[[2gyt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2gyt' size='340' side='right'caption='[[2gyt]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2gyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GYT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2gyt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GYT FirstGlance]. <br>
-</td></tr><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=2gyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gyt OCA], [http://pdbe.org/2gyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gyt RCSB], [http://www.ebi.ac.uk/pdbsum/2gyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gyt ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gyt OCA], [https://pdbe.org/2gyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gyt RCSB], [https://www.ebi.ac.uk/pdbsum/2gyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gyt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RHG07_HUMAN RHG07_HUMAN]] Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality.<ref>PMID:18786931</ref> <ref>PMID:19170769</ref> <ref>PMID:19710422</ref>
+[https://www.uniprot.org/uniprot/RHG07_HUMAN RHG07_HUMAN] Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality.<ref>PMID:18786931</ref> <ref>PMID:19170769</ref> <ref>PMID:19710422</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Yang, S]]
+[[Category: Large Structures]]
-[[Category: Protein binding]]
+[[Category: Yang S]]
-[[Category: Protein structure]]
-[[Category: Sam domain]]

2gyt

From Proteopedia

Current revision

Solution structure of the SAM (sterile alpha motif) domain of DLC1 (deleted in liver cancer 1)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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