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| | <StructureSection load='3co1' size='340' side='right'caption='[[3co1]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='3co1' size='340' side='right'caption='[[3co1]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3co1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CO1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CO1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3co1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CO1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pa7|1pa7]], [[1wyo|1wyo]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3co1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3co1 OCA], [http://pdbe.org/3co1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3co1 RCSB], [http://www.ebi.ac.uk/pdbsum/3co1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3co1 ProSAT]</span></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=3co1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3co1 OCA], [https://pdbe.org/3co1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3co1 RCSB], [https://www.ebi.ac.uk/pdbsum/3co1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3co1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MARE3_HUMAN MARE3_HUMAN]] Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).<ref>PMID:19255245</ref> | + | [https://www.uniprot.org/uniprot/MARE3_HUMAN MARE3_HUMAN] Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).<ref>PMID:19255245</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Groot, C O.De]] | + | [[Category: De Groot CO]] |
| - | [[Category: Honnappa, S]] | + | [[Category: Honnappa S]] |
| - | [[Category: Steinmetz, M O]] | + | [[Category: Steinmetz MO]] |
| - | [[Category: Tip protein]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Ch domain]]
| + | |
| - | [[Category: Microtubule-binding]]
| + | |
| - | [[Category: Mitosis]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Rp/eb family]]
| + | |
| Structural highlights
Function
MARE3_HUMAN Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).[1]
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
End binding proteins (EBs) are highly conserved core components of microtubule plus-end tracking protein networks. Here we investigated the roles of the three mammalian EBs in controlling microtubule dynamics and analyzed the domains involved. Protein depletion and rescue experiments showed that EB1 and EB3, but not EB2, promote persistent microtubule growth by suppressing catastrophes. Furthermore, we demonstrated in vitro and in cells that the EB plus-end tracking behavior depends on the calponin homology domain but does not require dimer formation. In contrast, dimerization is necessary for the EB anti-catastrophe activity in cells; this explains why the EB1 dimerization domain, which disrupts native EB dimers, exhibits a dominant-negative effect. When microtubule dynamics is reconstituted with purified tubulin, EBs promote rather than inhibit catastrophes, suggesting that in cells EBs prevent catastrophes by counteracting other microtubule regulators. This probably occurs through their action on microtubule ends, because catastrophe suppression does not require the EB domains needed for binding to known EB partners.
Mammalian end binding proteins control persistent microtubule growth.,Komarova Y, De Groot CO, Grigoriev I, Gouveia SM, Munteanu EL, Schober JM, Honnappa S, Buey RM, Hoogenraad CC, Dogterom M, Borisy GG, Steinmetz MO, Akhmanova A J Cell Biol. 2009 Mar 9;184(5):691-706. Epub 2009 Mar 2. PMID:19255245[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Komarova Y, De Groot CO, Grigoriev I, Gouveia SM, Munteanu EL, Schober JM, Honnappa S, Buey RM, Hoogenraad CC, Dogterom M, Borisy GG, Steinmetz MO, Akhmanova A. Mammalian end binding proteins control persistent microtubule growth. J Cell Biol. 2009 Mar 9;184(5):691-706. Epub 2009 Mar 2. PMID:19255245 doi:10.1083/jcb.200807179
- ↑ Komarova Y, De Groot CO, Grigoriev I, Gouveia SM, Munteanu EL, Schober JM, Honnappa S, Buey RM, Hoogenraad CC, Dogterom M, Borisy GG, Steinmetz MO, Akhmanova A. Mammalian end binding proteins control persistent microtubule growth. J Cell Biol. 2009 Mar 9;184(5):691-706. Epub 2009 Mar 2. PMID:19255245 doi:10.1083/jcb.200807179
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