3woy

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(Difference between revisions)

Revision as of 05:44, 3 August 2022

Crystal structure of CLASP2 TOG domain (TOG2)

Structural highlights

3woy is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3woz
Gene:	CLASP2, KIAA0627 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CLAP2_HUMAN] Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

CLIP-associated proteins CLASPs are mammalian microtubule (MT) plus-end tracking proteins (+TIPs) that promote MT rescue in vivo. Their plus-end localization is dependent on other +TIPs, EB1 and CLIP-170, but in the leading edge of the cell, CLASPs display lattice-binding activity. MT association of CLASPs is suggested to be regulated by multiple TOG (tumor overexpressed gene) domains and by the serine-arginine (SR)-rich region, which contains binding sites for EB1. Here, we report the crystal structures of the two TOG domains of CLASP2. Both domains consist of six HEAT repeats, which are similar to the canonical paddle-like tubulin-binding TOG domains, but have arched conformations. The degrees and directions of curvature are different between the two TOG domains, implying that they have distinct roles in MT binding. Using biochemical, molecular modeling and cell biological analyses, we have investigated the interactions between the TOG domains and alphabeta-tubulin and found that each domain associates differently with alphabeta-tubulin. Our findings suggest that, by varying the degrees of domain curvature, the TOG domains may distinguish the structural conformation of the tubulin dimer, discriminate between different states of MT dynamic instability and thereby function differentially as stabilizers of MTs.

CLASP2 Has Two Distinct TOG Domains That Contribute Differently to Microtubule Dynamics.,Maki T, Grimaldi AD, Fuchigami S, Kaverina I, Hayashi I J Mol Biol. 2015 Jul 17;427(14):2379-95. doi: 10.1016/j.jmb.2015.05.012. Epub, 2015 May 21. PMID:26003921^[8]

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

References

↑ Akhmanova A, Hoogenraad CC, Drabek K, Stepanova T, Dortland B, Verkerk T, Vermeulen W, Burgering BM, De Zeeuw CI, Grosveld F, Galjart N. Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts. Cell. 2001 Mar 23;104(6):923-35. PMID:11290329
↑ Mimori-Kiyosue Y, Grigoriev I, Lansbergen G, Sasaki H, Matsui C, Severin F, Galjart N, Grosveld F, Vorobjev I, Tsukita S, Akhmanova A. CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex. J Cell Biol. 2005 Jan 3;168(1):141-53. PMID:15631994 doi:10.1083/jcb.200405094
↑ Lansbergen G, Grigoriev I, Mimori-Kiyosue Y, Ohtsuka T, Higa S, Kitajima I, Demmers J, Galjart N, Houtsmuller AB, Grosveld F, Akhmanova A. CLASPs attach microtubule plus ends to the cell cortex through a complex with LL5beta. Dev Cell. 2006 Jul;11(1):21-32. PMID:16824950 doi:http://dx.doi.org/S1534-5807(06)00252-8
↑ Mimori-Kiyosue Y, Grigoriev I, Sasaki H, Matsui C, Akhmanova A, Tsukita S, Vorobjev I. Mammalian CLASPs are required for mitotic spindle organization and kinetochore alignment. Genes Cells. 2006 Aug;11(8):845-57. PMID:16866869 doi:GTC990
↑ Pereira AL, Pereira AJ, Maia AR, Drabek K, Sayas CL, Hergert PJ, Lince-Faria M, Matos I, Duque C, Stepanova T, Rieder CL, Earnshaw WC, Galjart N, Maiato H. Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by regulating spindle and kinetochore function. Mol Biol Cell. 2006 Oct;17(10):4526-42. Epub 2006 Aug 16. PMID:16914514 doi:E06-07-0579
↑ Efimov A, Kharitonov A, Efimova N, Loncarek J, Miller PM, Andreyeva N, Gleeson P, Galjart N, Maia AR, McLeod IX, Yates JR 3rd, Maiato H, Khodjakov A, Akhmanova A, Kaverina I. Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network. Dev Cell. 2007 Jun;12(6):917-30. PMID:17543864 doi:10.1016/j.devcel.2007.04.002
↑ Zaoui K, Benseddik K, Daou P, Salaun D, Badache A. ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18517-22. doi:, 10.1073/pnas.1000975107. Epub 2010 Oct 11. PMID:20937854 doi:10.1073/pnas.1000975107
↑ Maki T, Grimaldi AD, Fuchigami S, Kaverina I, Hayashi I. CLASP2 Has Two Distinct TOG Domains That Contribute Differently to Microtubule Dynamics. J Mol Biol. 2015 Jul 17;427(14):2379-95. doi: 10.1016/j.jmb.2015.05.012. Epub, 2015 May 21. PMID:26003921 doi:http://dx.doi.org/10.1016/j.jmb.2015.05.012

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of CLASP2 TOG domain (TOG2)==
-<StructureSection load='3woy' size='340' side='right' caption='[[3woy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='3woy' size='340' side='right'caption='[[3woy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3woy]] 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=3WOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WOY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3woy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WOY FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3woz|3woz]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3woz|3woz]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLASP2, KIAA0627 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLASP2, KIAA0627 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3woy OCA], [http://pdbe.org/3woy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3woy RCSB], [http://www.ebi.ac.uk/pdbsum/3woy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3woy 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=3woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3woy OCA], [https://pdbe.org/3woy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3woy RCSB], [https://www.ebi.ac.uk/pdbsum/3woy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3woy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CLAP2_HUMAN CLAP2_HUMAN]] Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.<ref>PMID:11290329</ref> <ref>PMID:15631994</ref> <ref>PMID:16824950</ref> <ref>PMID:16866869</ref> <ref>PMID:16914514</ref> <ref>PMID:17543864</ref> <ref>PMID:20937854</ref>
+[[https://www.uniprot.org/uniprot/CLAP2_HUMAN CLAP2_HUMAN]] Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.<ref>PMID:11290329</ref> <ref>PMID:15631994</ref> <ref>PMID:16824950</ref> <ref>PMID:16866869</ref> <ref>PMID:16914514</ref> <ref>PMID:17543864</ref> <ref>PMID:20937854</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Hayashi, I]]
 [[Category: Maki, T]]

3woy

From Proteopedia

Revision as of 05:44, 3 August 2022

Crystal structure of CLASP2 TOG domain (TOG2)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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