4wjw

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of the Chs5-Chs6 Exomer Cargo Adaptor Complex Bound to portion of Chs3

Structural highlights

4wjw is a 3 chain structure with sequence from Saccharomyces cerevisiae and Saccharomyces cerevisiae S288C. This structure supersedes the now removed PDB entry 4u9t. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.59Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHS5_YEAST Component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. Also involved in targeting FUS1 to sites of polarized growth.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Publication Abstract from PubMed

Cells transport integral membrane proteins between organelles by sorting them into vesicles. Cargo adaptors act to recognize sorting signals in transmembrane cargos and to interact with coat complexes that aid in vesicle biogenesis. No coat proteins have yet been identified that generate secretory vesicles from the trans-Golgi network (TGN) to the plasma membrane, but the exomer complex has been identified as a cargo adaptor complex that mediates transport of several proteins in this pathway. Chs3, the most well-studied exomer cargo, cycles between the TGN and the plasma membrane in synchrony with the cell cycle, providing an opportunity to study regulation of proteins that cycle in response to signaling. Here we show that different segments of the Chs3 N-terminus mediate distinct trafficking steps. Residues 10-27, known to mediate retention, also appear to play a role in internalization. Residues 28-52 are involved in transport to the plasma membrane and recycling out of endosomes to prevent degradation in the vacuole. We also present the crystal structure of residues 10-27 bound to the exomer complex, suggesting different cargo adaptors could compete for binding to this segment, providing a potential mechanism for regulation.

Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary.,Weiskoff AM, Fromme JC Front Cell Dev Biol. 2014 Sep 3;2:47. doi: 10.3389/fcell.2014.00047. eCollection , 2014. PMID:25364754^[9]

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

References

↑ Santos B, Duran A, Valdivieso MH. CHS5, a gene involved in chitin synthesis and mating in Saccharomyces cerevisiae. Mol Cell Biol. 1997 May;17(5):2485-96. PMID:9111317
↑ Choi WJ, Sburlati A, Cabib E. Chitin synthase 3 from yeast has zymogenic properties that depend on both the CAL1 and the CAL3 genes. Proc Natl Acad Sci U S A. 1994 May 24;91(11):4727-30. PMID:8197125
↑ Santos B, Snyder M. Specific protein targeting during cell differentiation: polarized localization of Fus1p during mating depends on Chs5p in Saccharomyces cerevisiae. Eukaryot Cell. 2003 Aug;2(4):821-5. PMID:12912901
↑ Lesage G, Shapiro J, Specht CA, Sdicu AM, Menard P, Hussein S, Tong AH, Boone C, Bussey H. An interactional network of genes involved in chitin synthesis in Saccharomyces cerevisiae. BMC Genet. 2005 Feb 16;6:8. PMID:15715908 doi:10.1186/1471-2156-6-8
↑ Trautwein M, Schindler C, Gauss R, Dengjel J, Hartmann E, Spang A. Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi. EMBO J. 2006 Mar 8;25(5):943-54. Epub 2006 Feb 23. PMID:16498409 doi:7601007
↑ Lam KK, Davey M, Sun B, Roth AF, Davis NG, Conibear E. Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3. J Cell Biol. 2006 Jul 3;174(1):19-25. PMID:16818716 doi:jcb.200602049
↑ Wang CW, Hamamoto S, Orci L, Schekman R. Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast. J Cell Biol. 2006 Sep 25;174(7):973-83. PMID:17000877 doi:10.1083/jcb.200605106
↑ Sanchatjate S, Schekman R. Chs5/6 complex: a multiprotein complex that interacts with and conveys chitin synthase III from the trans-Golgi network to the cell surface. Mol Biol Cell. 2006 Oct;17(10):4157-66. Epub 2006 Jul 19. PMID:16855022 doi:10.1091/mbc.E06-03-0210
↑ Weiskoff AM, Fromme JC. Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary. Front Cell Dev Biol. 2014 Sep 3;2:47. doi: 10.3389/fcell.2014.00047. eCollection , 2014. PMID:25364754 doi:http://dx.doi.org/10.3389/fcell.2014.00047

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/4wjw"

Categories: Large Structures | Saccharomyces cerevisiae | Saccharomyces cerevisiae S288C | Fromme JC | Weiskoff AM

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4wjw is ON HOLD
+==Crystal Structure of the Chs5-Chs6 Exomer Cargo Adaptor Complex Bound to portion of Chs3==
+<StructureSection load='4wjw' size='340' side='right'caption='[[4wjw]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4wjw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4u9t 4u9t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WJW 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]] 2.59&#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=4wjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wjw OCA], [https://pdbe.org/4wjw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wjw RCSB], [https://www.ebi.ac.uk/pdbsum/4wjw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wjw ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHS5_YEAST CHS5_YEAST] Component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. Also involved in targeting FUS1 to sites of polarized growth.<ref>PMID:9111317</ref> <ref>PMID:8197125</ref> <ref>PMID:12912901</ref> <ref>PMID:15715908</ref> <ref>PMID:16498409</ref> <ref>PMID:16818716</ref> <ref>PMID:17000877</ref> <ref>PMID:16855022</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cells transport integral membrane proteins between organelles by sorting them into vesicles. Cargo adaptors act to recognize sorting signals in transmembrane cargos and to interact with coat complexes that aid in vesicle biogenesis. No coat proteins have yet been identified that generate secretory vesicles from the trans-Golgi network (TGN) to the plasma membrane, but the exomer complex has been identified as a cargo adaptor complex that mediates transport of several proteins in this pathway. Chs3, the most well-studied exomer cargo, cycles between the TGN and the plasma membrane in synchrony with the cell cycle, providing an opportunity to study regulation of proteins that cycle in response to signaling. Here we show that different segments of the Chs3 N-terminus mediate distinct trafficking steps. Residues 10-27, known to mediate retention, also appear to play a role in internalization. Residues 28-52 are involved in transport to the plasma membrane and recycling out of endosomes to prevent degradation in the vacuole. We also present the crystal structure of residues 10-27 bound to the exomer complex, suggesting different cargo adaptors could compete for binding to this segment, providing a potential mechanism for regulation.
-Authors: Weiskoff, A.M., Fromme, J.C.
+Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary.,Weiskoff AM, Fromme JC Front Cell Dev Biol. 2014 Sep 3;2:47. doi: 10.3389/fcell.2014.00047. eCollection , 2014. PMID:25364754<ref>PMID:25364754</ref>
-Description: Crystal Structure of the Chs5-Chs6 Exomer Cargo Adaptor Complex Bound to portion of Chs3
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4wjw" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Fromme JC]]
+[[Category: Weiskoff AM]]

4wjw

From Proteopedia

Current revision

Crystal Structure of the Chs5-Chs6 Exomer Cargo Adaptor Complex Bound to portion of Chs3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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