7z8j: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7z8j]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z8J FirstGlance]. <br>
<table><tr><td colspan='2'>[[7z8j]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z8J FirstGlance]. <br>
</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=7z8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z8j OCA], [https://pdbe.org/7z8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z8j RCSB], [https://www.ebi.ac.uk/pdbsum/7z8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z8j ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.93&#8491;</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=7z8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z8j OCA], [https://pdbe.org/7z8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z8j RCSB], [https://www.ebi.ac.uk/pdbsum/7z8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z8j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/BICL1_MOUSE BICL1_MOUSE] Component of secretory vesicle machinery in developing neurons that acts as a regulator of neurite outgrowth. Regulates the secretory vesicle transport by controlling the accumulation of Rab6-containing secretory vesicles in the pericentrosomal region restricting anterograde secretory transport during the early phase of neuronal differentiation, thereby inhibiting neuritogenesis.<ref>PMID:20360680</ref>  
[https://www.uniprot.org/uniprot/BICL1_MOUSE BICL1_MOUSE] Component of secretory vesicle machinery in developing neurons that acts as a regulator of neurite outgrowth. Regulates the secretory vesicle transport by controlling the accumulation of Rab6-containing secretory vesicles in the pericentrosomal region restricting anterograde secretory transport during the early phase of neuronal differentiation, thereby inhibiting neuritogenesis.<ref>PMID:20360680</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor(1-3). Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour(4-6). Different coiled-coil adaptors are linked to different cargos(7,8), and some share motifs known to contact sites on dynein and dynactin(4,9-13). There is limited structural information on how the resulting complex interacts with microtubules and how adaptors are recruited. Here we develop a cryo-electron microscopy processing pipeline to solve the high-resolution structure of dynein-dynactin and the adaptor BICDR1 bound to microtubules. This reveals the asymmetric interactions between neighbouring dynein motor domains and how they relate to motile behaviour. We found that two adaptors occupy the complex. Both adaptors make similar interactions with the dyneins but diverge in their contacts with each other and dynactin. Our structure has implications for the stability and stoichiometry of motor recruitment by cargos.
Structure of dynein-dynactin on microtubules shows tandem adaptor binding.,Chaaban S, Carter AP Nature. 2022 Oct;610(7930):212-216. doi: 10.1038/s41586-022-05186-y. Epub 2022 , Sep 7. PMID:36071160<ref>PMID:36071160</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7z8j" style="background-color:#fffaf0;"></div>
==See Also==
*[[Dynein 3D structures|Dynein 3D structures]]
== References ==
== References ==
<references/>
<references/>

Latest revision as of 09:40, 24 July 2024

Cytoplasmic dynein (A2) bound to BICDR1Cytoplasmic dynein (A2) bound to BICDR1

Structural highlights

7z8j is a 9 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.93Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BICL1_MOUSE Component of secretory vesicle machinery in developing neurons that acts as a regulator of neurite outgrowth. Regulates the secretory vesicle transport by controlling the accumulation of Rab6-containing secretory vesicles in the pericentrosomal region restricting anterograde secretory transport during the early phase of neuronal differentiation, thereby inhibiting neuritogenesis.[1]

Publication Abstract from PubMed

Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor(1-3). Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour(4-6). Different coiled-coil adaptors are linked to different cargos(7,8), and some share motifs known to contact sites on dynein and dynactin(4,9-13). There is limited structural information on how the resulting complex interacts with microtubules and how adaptors are recruited. Here we develop a cryo-electron microscopy processing pipeline to solve the high-resolution structure of dynein-dynactin and the adaptor BICDR1 bound to microtubules. This reveals the asymmetric interactions between neighbouring dynein motor domains and how they relate to motile behaviour. We found that two adaptors occupy the complex. Both adaptors make similar interactions with the dyneins but diverge in their contacts with each other and dynactin. Our structure has implications for the stability and stoichiometry of motor recruitment by cargos.

Structure of dynein-dynactin on microtubules shows tandem adaptor binding.,Chaaban S, Carter AP Nature. 2022 Oct;610(7930):212-216. doi: 10.1038/s41586-022-05186-y. Epub 2022 , Sep 7. PMID:36071160[2]

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

See Also

References

  1. ↑ Schlager MA, Kapitein LC, Grigoriev I, Burzynski GM, Wulf PS, Keijzer N, de Graaff E, Fukuda M, Shepherd IT, Akhmanova A, Hoogenraad CC. Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis. EMBO J. 2010 May 19;29(10):1637-51. doi: 10.1038/emboj.2010.51. Epub 2010 Apr 1. PMID:20360680 doi:http://dx.doi.org/10.1038/emboj.2010.51
  2. ↑ Chaaban S, Carter AP. Structure of dynein-dynactin on microtubules shows tandem adaptor binding. Nature. 2022 Sep 7. pii: 10.1038/s41586-022-05186-y. doi:, 10.1038/s41586-022-05186-y. PMID:36071160 doi:http://dx.doi.org/10.1038/s41586-022-05186-y

7z8j, resolution 3.93Å

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