7y8w

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of DLC-1/SAO-1 complex

Structural highlights

7y8w is a 20 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DYL1_CAEEL Acts as a non-catalytic accessory component of a dynein complex (By similarity). Part of a complex with bicd-1 and egal-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migrations in hypodermal precursor cells (PubMed:20005871). Probably within a dynein motor complex, plays a role in the cell fate specification of the germline and oogenesis (PubMed:19752194, PubMed:27864381). In particular, it inhibits germ cell proliferation (PubMed:19752194). Regulates the function and localization of the RNA-binding protein fbf-2 in the germline (PubMed:27864381). Plays a role in mitotic and meiotic processes (PubMed:19752194, PubMed:26483555). Involved in the pairing of homologous chromosomes (PubMed:26483555). Independently of its dynein-mediated functions, plays a role in germ cell apoptosis (PubMed:24030151).[UniProtKB:Q24117]^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Apoptosis is one of the major forms of programmed cell death, and it serves vital biological functions in multicellular animal and plant cells. The core mechanism of apoptosis is highly conserved in metazoans, where the translocation of CED-4/Apaf-1 from mitochondria to the nuclear membrane is required to initiate and execute apoptosis. However, the underlying molecular mechanisms of this translocation are poorly understood. In this study, we showed that SAO-1 binds DLC-1 and prevents its degradation to promote apoptosis in C. elegans germ cells. We demonstrated that SAO-1 and DLC-1 regulate CED-4/Apaf-1 nuclear membrane accumulation during apoptosis. Isothermal titration calorimetry-based assay and high-resolution crystal structure analysis further revealed that SAO-1 interacted with DLC-1 to form a 2:4 complex: each of the two beta-sheets in the SAO-1 peptide interacted with two DLC-1 dimers. Point mutations at the SAO-1-DLC-1 binding interface significantly inhibited apoptotic corpse formation and CED-4 nuclear membrane accumulation within C. elegans germ cells. In conclusion, our study provides a new perspective on the regulation of CED-4-mediated apoptosis.

Interaction between DLC-1 and SAO-1 facilitates CED-4 translocation during apoptosis in the Caenorhabditis elegans germline.,Zhang D, Yang H, Jiang L, Zhao C, Wang M, Hu B, Yu C, Wei Z, Tse YC Cell Death Discov. 2022 Nov 3;8(1):441. doi: 10.1038/s41420-022-01233-9. PMID:36323675^[6]

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

References

↑ Dorsett M, Schedl T. A role for dynein in the inhibition of germ cell proliferative fate. Mol Cell Biol. 2009 Nov;29(22):6128-39. doi: 10.1128/MCB.00815-09. Epub 2009 Sep , 14. PMID:19752194 doi:http://dx.doi.org/10.1128/MCB.00815-09
↑ Fridolfsson HN, Ly N, Meyerzon M, Starr DA. UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope during nuclear migration. Dev Biol. 2010 Feb 15;338(2):237-50. PMID:20005871 doi:10.1016/j.ydbio.2009.12.004
↑ Morthorst TH, Olsen A. Cell-nonautonomous inhibition of radiation-induced apoptosis by dynein light chain 1 in Caenorhabditis elegans. Cell Death Dis. 2013 Sep 12;4(9):e799. PMID:24030151 doi:10.1038/cddis.2013.319
↑ Bohr T, Nelson CR, Klee E, Bhalla N. Spindle assembly checkpoint proteins regulate and monitor meiotic synapsis in C. elegans. J Cell Biol. 2015 Oct 26;211(2):233-42. PMID:26483555 doi:10.1083/jcb.201409035
↑ Wang X, Olson JR, Rasoloson D, Ellenbecker M, Bailey J, Voronina E. Dynein light chain DLC-1 promotes localization and function of the PUF protein FBF-2 in germline progenitor cells. Development. 2016 Dec 15;143(24):4643-4653. PMID:27864381 doi:10.1242/dev.140921
↑ Zhang D, Yang H, Jiang L, Zhao C, Wang M, Hu B, Yu C, Wei Z, Tse YC. Interaction between DLC-1 and SAO-1 facilitates CED-4 translocation during apoptosis in the Caenorhabditis elegans germline. Cell Death Discov. 2022 Nov 3;8(1):441. PMID:36323675 doi:10.1038/s41420-022-01233-9

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/7y8w"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7y8w is ON HOLD
+==Crystal structure of DLC-1/SAO-1 complex==
+<StructureSection load='7y8w' size='340' side='right'caption='[[7y8w]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7y8w]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y8W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y8W 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]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=7y8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y8w OCA], [https://pdbe.org/7y8w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y8w RCSB], [https://www.ebi.ac.uk/pdbsum/7y8w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y8w ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DYL1_CAEEL DYL1_CAEEL] Acts as a non-catalytic accessory component of a dynein complex (By similarity). Part of a complex with bicd-1 and egal-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migrations in hypodermal precursor cells (PubMed:20005871). Probably within a dynein motor complex, plays a role in the cell fate specification of the germline and oogenesis (PubMed:19752194, PubMed:27864381). In particular, it inhibits germ cell proliferation (PubMed:19752194). Regulates the function and localization of the RNA-binding protein fbf-2 in the germline (PubMed:27864381). Plays a role in mitotic and meiotic processes (PubMed:19752194, PubMed:26483555). Involved in the pairing of homologous chromosomes (PubMed:26483555). Independently of its dynein-mediated functions, plays a role in germ cell apoptosis (PubMed:24030151).[UniProtKB:Q24117]<ref>PMID:19752194</ref> <ref>PMID:20005871</ref> <ref>PMID:24030151</ref> <ref>PMID:26483555</ref> <ref>PMID:27864381</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Apoptosis is one of the major forms of programmed cell death, and it serves vital biological functions in multicellular animal and plant cells. The core mechanism of apoptosis is highly conserved in metazoans, where the translocation of CED-4/Apaf-1 from mitochondria to the nuclear membrane is required to initiate and execute apoptosis. However, the underlying molecular mechanisms of this translocation are poorly understood. In this study, we showed that SAO-1 binds DLC-1 and prevents its degradation to promote apoptosis in C. elegans germ cells. We demonstrated that SAO-1 and DLC-1 regulate CED-4/Apaf-1 nuclear membrane accumulation during apoptosis. Isothermal titration calorimetry-based assay and high-resolution crystal structure analysis further revealed that SAO-1 interacted with DLC-1 to form a 2:4 complex: each of the two beta-sheets in the SAO-1 peptide interacted with two DLC-1 dimers. Point mutations at the SAO-1-DLC-1 binding interface significantly inhibited apoptotic corpse formation and CED-4 nuclear membrane accumulation within C. elegans germ cells. In conclusion, our study provides a new perspective on the regulation of CED-4-mediated apoptosis.
-Authors:
+Interaction between DLC-1 and SAO-1 facilitates CED-4 translocation during apoptosis in the Caenorhabditis elegans germline.,Zhang D, Yang H, Jiang L, Zhao C, Wang M, Hu B, Yu C, Wei Z, Tse YC Cell Death Discov. 2022 Nov 3;8(1):441. doi: 10.1038/s41420-022-01233-9. PMID:36323675<ref>PMID:36323675</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7y8w" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Caenorhabditis elegans]]
+[[Category: Large Structures]]
+[[Category: Wei Z]]
+[[Category: Yan H]]
+[[Category: Yu C]]
+[[Category: Zhao C]]

7y8w

From Proteopedia

Current revision

Crystal structure of DLC-1/SAO-1 complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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