2qk2

From Proteopedia

(Difference between revisions)

Current revision

Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1

Structural highlights

2qk2 is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MSPS_DROME Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. May act as a microtubule antipause factor that rapidly catalyzes the transition from pause to either growth or shrinkage. Involved in mitotic spindle elongation. Involved in the establishment of cell polarity and mitotic spindle orientation in neuroblasts. Required for maintaining the bipolarity of acentrosomal meiotic spindles; the function is dependent on tacc and involves ncd. Involved in oocyte microtubule cytoskeleton organization and bicoid mRNA localization. Seems to be involved in elongation of kinetochore-derived microtubule fibers.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

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

Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170), but whether they act upon microtubule plus ends through a similar mechanism has not been resolved. Here, we report crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p and Drosophila Msps), EB1 (yeast Bim1p and human EB1), and CLIP-170 (human), which reveal diverse tubulin binding interfaces. Functional studies, however, reveal a common property that native or artificial dimerization of tubulin binding domains (including chemically induced heterodimers of EB1 and CLIP-170) induces tubulin nucleation/assembly in vitro and, in most cases, plus end tracking in living cells. We propose that +TIPs, although diverse in structure, share a common property of multimerizing tubulin, thus acting as polymerization chaperones that aid in subunit addition to the microtubule plus end.

Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1.,Slep KC, Vale RD Mol Cell. 2007 Sep 21;27(6):976-91. PMID:17889670^[9]

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

References

↑ Cullen CF, Deak P, Glover DM, Ohkura H. mini spindles: A gene encoding a conserved microtubule-associated protein required for the integrity of the mitotic spindle in Drosophila. J Cell Biol. 1999 Sep 6;146(5):1005-18. PMID:10477755
↑ Cullen CF, Ohkura H. Msps protein is localized to acentrosomal poles to ensure bipolarity of Drosophila meiotic spindles. Nat Cell Biol. 2001 Jul;3(7):637-42. PMID:11433295 doi:http://dx.doi.org/10.1038/35083025
↑ Moon W, Hazelrigg T. The Drosophila microtubule-associated protein mini spindles is required for cytoplasmic microtubules in oogenesis. Curr Biol. 2004 Nov 9;14(21):1957-61. PMID:15530399 doi:http://dx.doi.org/10.1016/j.cub.2004.10.023
↑ Brittle AL, Ohkura H. Mini spindles, the XMAP215 homologue, suppresses pausing of interphase microtubules in Drosophila. EMBO J. 2005 Apr 6;24(7):1387-96. Epub 2005 Mar 17. PMID:15775959 doi:http://dx.doi.org/10.1038/sj.emboj.7600629
↑ Goshima G, Wollman R, Stuurman N, Scholey JM, Vale RD. Length control of the metaphase spindle. Curr Biol. 2005 Nov 22;15(22):1979-88. PMID:16303556 doi:10.1016/j.cub.2005.09.054
↑ Slep KC, Vale RD. Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1. Mol Cell. 2007 Sep 21;27(6):976-91. PMID:17889670 doi:10.1016/j.molcel.2007.07.023
↑ Chen K, Koe CT, Xing ZB, Tian X, Rossi F, Wang C, Tang Q, Zong W, Hong WJ, Taneja R, Yu F, Gonzalez C, Wu C, Endow S, Wang H. Arl2- and Msps-dependent microtubule growth governs asymmetric division. J Cell Biol. 2016 Mar 14;212(6):661-76. doi: 10.1083/jcb.201503047. Epub 2016 Mar, 7. PMID:26953351 doi:http://dx.doi.org/10.1083/jcb.201503047
↑ Currie JD, Stewman S, Schimizzi G, Slep KC, Ma A, Rogers SL. The microtubule lattice and plus-end association of Drosophila Mini spindles is spatially regulated to fine-tune microtubule dynamics. Mol Biol Cell. 2011 Nov;22(22):4343-61. doi: 10.1091/mbc.E11-06-0520. Epub 2011, Sep 30. PMID:21965297 doi:http://dx.doi.org/10.1091/mbc.E11-06-0520
↑ Slep KC, Vale RD. Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1. Mol Cell. 2007 Sep 21;27(6):976-91. PMID:17889670 doi:10.1016/j.molcel.2007.07.023

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/2qk2"

Categories: Drosophila melanogaster | Large Structures | Slep KC | Vale RD

@@ Line 3: / Line 3: @@
 <StructureSection load='2qk2' size='340' side='right'caption='[[2qk2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2qk2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QK2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2qk2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QK2 FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qjx|2qjx]], [[2qjz|2qjz]], [[2qk0|2qk0]], [[2qk1|2qk1]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msps ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=2qk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qk2 OCA], [https://pdbe.org/2qk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qk2 RCSB], [https://www.ebi.ac.uk/pdbsum/2qk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qk2 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MSPS_DROME MSPS_DROME] Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. May act as a microtubule antipause factor that rapidly catalyzes the transition from pause to either growth or shrinkage. Involved in mitotic spindle elongation. Involved in the establishment of cell polarity and mitotic spindle orientation in neuroblasts. Required for maintaining the bipolarity of acentrosomal meiotic spindles; the function is dependent on tacc and involves ncd. Involved in oocyte microtubule cytoskeleton organization and bicoid mRNA localization. Seems to be involved in elongation of kinetochore-derived microtubule fibers.<ref>PMID:10477755</ref> <ref>PMID:11433295</ref> <ref>PMID:15530399</ref> <ref>PMID:15775959</ref> <ref>PMID:16303556</ref> <ref>PMID:17889670</ref> <ref>PMID:26953351</ref> <ref>PMID:21965297</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/2qk2_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
 [[Category: Large Structures]]
-[[Category: Slep, K C]]
+[[Category: Slep KC]]
-[[Category: Vale, R D]]
+[[Category: Vale RD]]
-[[Category: Tip]]
-[[Category: Dis1]]
-[[Category: Heat repeat]]
-[[Category: Microtubule plus end]]
-[[Category: Mini spindle]]
-[[Category: Msp]]
-[[Category: Protein binding]]
-[[Category: Stu2]]
-[[Category: Xmap215]]

2qk2

From Proteopedia

Current revision

Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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