5nbt: Difference between revisions
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==Apo structure of p60N/p80C katanin== | |||
<StructureSection load='5nbt' size='340' side='right'caption='[[5nbt]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nbt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NBT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=5nbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbt OCA], [https://pdbe.org/5nbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nbt RCSB], [https://www.ebi.ac.uk/pdbsum/5nbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KTNB1_MOUSE KTNB1_MOUSE] Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.[HAMAP-Rule:MF_03022] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ASPM (known as Asp in fly and ASPM-1 in worm) is a microcephaly-associated protein family that regulates spindle architecture, but the underlying mechanism is poorly understood. Here, we show that ASPM forms a complex with another protein linked to microcephaly, the microtubule-severing ATPase katanin. ASPM and katanin localize to spindle poles in a mutually dependent manner and regulate spindle flux. X-ray crystallography revealed that the heterodimer formed by the N- and C-terminal domains of the katanin subunits p60 and p80, respectively, binds conserved motifs in ASPM. Reconstitution experiments demonstrated that ASPM autonomously tracks growing microtubule minus ends and inhibits their growth, while katanin decorates and bends both ends of dynamic microtubules and potentiates the minus-end blocking activity of ASPM. ASPM also binds along microtubules, recruits katanin and promotes katanin-mediated severing of dynamic microtubules. We propose that the ASPM-katanin complex controls microtubule disassembly at spindle poles and that misregulation of this process can lead to microcephaly. | |||
Microtubule minus-end regulation at spindle poles by an ASPM-katanin complex.,Jiang K, Rezabkova L, Hua S, Liu Q, Capitani G, Maarten Altelaar AF, Heck AJR, Kammerer RA, Steinmetz MO, Akhmanova A Nat Cell Biol. 2017 May;19(5):480-492. doi: 10.1038/ncb3511. Epub 2017 Apr 24. PMID:28436967<ref>PMID:28436967</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5nbt" style="background-color:#fffaf0;"></div> | ||
[[Category: Akhmanova | == References == | ||
[[Category: | <references/> | ||
[[Category: Heck | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Akhmanova A]] | ||
[[Category: | [[Category: Altelaar AFM]] | ||
[[Category: | [[Category: Capitani G]] | ||
[[Category: Heck AJR]] | |||
[[Category: Hua S]] | |||
[[Category: Jiang K]] | |||
[[Category: Kammerer RA]] | |||
[[Category: Liu Q]] | |||
[[Category: Rezabkova L]] | |||
[[Category: Steinmetz MO]] | |||
Latest revision as of 15:45, 15 November 2023
Apo structure of p60N/p80C kataninApo structure of p60N/p80C katanin
Structural highlights
FunctionKTNB1_MOUSE Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.[HAMAP-Rule:MF_03022] Publication Abstract from PubMedASPM (known as Asp in fly and ASPM-1 in worm) is a microcephaly-associated protein family that regulates spindle architecture, but the underlying mechanism is poorly understood. Here, we show that ASPM forms a complex with another protein linked to microcephaly, the microtubule-severing ATPase katanin. ASPM and katanin localize to spindle poles in a mutually dependent manner and regulate spindle flux. X-ray crystallography revealed that the heterodimer formed by the N- and C-terminal domains of the katanin subunits p60 and p80, respectively, binds conserved motifs in ASPM. Reconstitution experiments demonstrated that ASPM autonomously tracks growing microtubule minus ends and inhibits their growth, while katanin decorates and bends both ends of dynamic microtubules and potentiates the minus-end blocking activity of ASPM. ASPM also binds along microtubules, recruits katanin and promotes katanin-mediated severing of dynamic microtubules. We propose that the ASPM-katanin complex controls microtubule disassembly at spindle poles and that misregulation of this process can lead to microcephaly. Microtubule minus-end regulation at spindle poles by an ASPM-katanin complex.,Jiang K, Rezabkova L, Hua S, Liu Q, Capitani G, Maarten Altelaar AF, Heck AJR, Kammerer RA, Steinmetz MO, Akhmanova A Nat Cell Biol. 2017 May;19(5):480-492. doi: 10.1038/ncb3511. Epub 2017 Apr 24. PMID:28436967[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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