8bbe

From Proteopedia

(Difference between revisions)

Revision as of 09:27, 21 December 2022

Structure of the IFT-A complex; IFT-A2 module

Structural highlights

8bbe is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

IFT43_HUMAN Cranioectodermal dysplasia. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.

Function

IFT43_HUMAN As a component of IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis (PubMed:28400947, PubMed:28973684). Involved in retrograde ciliary transport along microtubules from the ciliary tip to the base (PubMed:21378380).^[1] ^[2] ^[3]

Publication Abstract from PubMed

Intraflagellar transport (IFT) trains are massive molecular machines that traffic proteins between cilia and the cell body. Each IFT train is a dynamic polymer of two large complexes (IFT-A and -B) and motor proteins, posing a formidable challenge to mechanistic understanding. Here, we reconstituted the complete human IFT-A complex and obtained its structure using cryo-EM. Combined with AlphaFold prediction and genome-editing studies, our results illuminate how IFT-A polymerizes, interacts with IFT-B, and uses an array of beta-propeller and TPR domains to create "carriages" of the IFT train that engage TULP adaptor proteins. We show that IFT-AâTULP carriages are essential for cilia localization of diverse membrane proteins, as well as ICK-the key kinase regulating IFT train turnaround. These data establish a structural link between IFT-A's distinct functions, provide a blueprint for IFT-A in the train, and shed light on how IFT evolved from a proto-coatomer ancestor.

IFT-A structure reveals carriages for membrane protein transport into cilia.,Hesketh SJ, Mukhopadhyay AG, Nakamura D, Toropova K, Roberts AJ Cell. 2022 Nov 30:S0092-8674(22)01422-2. doi: 10.1016/j.cell.2022.11.010. PMID:36462505^[4]

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

References

↑ Arts HH, Bongers EM, Mans DA, van Beersum SE, Oud MM, Bolat E, Spruijt L, Cornelissen EA, Schuurs-Hoeijmakers JH, de Leeuw N, Cormier-Daire V, Brunner HG, Knoers NV, Roepman R. C14ORF179 encoding IFT43 is mutated in Sensenbrenner syndrome. J Med Genet. 2011 Jun;48(6):390-5. doi: 10.1136/jmg.2011.088864. Epub 2011 Mar 4. PMID:21378380 doi:http://dx.doi.org/10.1136/jmg.2011.088864
↑ Duran I, Taylor SP, Zhang W, Martin J, Qureshi F, Jacques SM, Wallerstein R, Lachman RS, Nickerson DA, Bamshad M, Cohn DH, Krakow D. Mutations in IFT-A satellite core component genes IFT43 and IFT121 produce short rib polydactyly syndrome with distinctive campomelia. Cilia. 2017 Apr 10;6:7. doi: 10.1186/s13630-017-0051-y. eCollection 2017. PMID:28400947 doi:http://dx.doi.org/10.1186/s13630-017-0051-y
↑ Biswas P, Duncan JL, Ali M, Matsui H, Naeem MA, Raghavendra PB, Frazer KA, Arts HH, Riazuddin S, Akram J, Hejtmancik JF, Riazuddin SA, Ayyagari R. A mutation in IFT43 causes non-syndromic recessive retinal degeneration. Hum Mol Genet. 2017 Dec 1;26(23):4741-4751. doi: 10.1093/hmg/ddx356. PMID:28973684 doi:http://dx.doi.org/10.1093/hmg/ddx356
↑ Hesketh SJ, Mukhopadhyay AG, Nakamura D, Toropova K, Roberts AJ. IFT-A structure reveals carriages for membrane protein transport into cilia. Cell. 2022 Nov 30:S0092-8674(22)01422-2. doi: 10.1016/j.cell.2022.11.010. PMID:36462505 doi:http://dx.doi.org/10.1016/j.cell.2022.11.010

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8bbe"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8bbe is ON HOLD
+==Structure of the IFT-A complex; IFT-A2 module==
+<StructureSection load='8bbe' size='340' side='right'caption='[[8bbe]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8bbe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BBE 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=8bbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bbe OCA], [https://pdbe.org/8bbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bbe RCSB], [https://www.ebi.ac.uk/pdbsum/8bbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bbe ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/IFT43_HUMAN IFT43_HUMAN] Cranioectodermal dysplasia. The disease is caused by variants affecting the gene represented in this entry.  The disease is caused by variants affecting the gene represented in this entry.  The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/IFT43_HUMAN IFT43_HUMAN] As a component of IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis (PubMed:28400947, PubMed:28973684). Involved in retrograde ciliary transport along microtubules from the ciliary tip to the base (PubMed:21378380).<ref>PMID:21378380</ref> <ref>PMID:28400947</ref> <ref>PMID:28973684</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Intraflagellar transport (IFT) trains are massive molecular machines that traffic proteins between cilia and the cell body. Each IFT train is a dynamic polymer of two large complexes (IFT-A and -B) and motor proteins, posing a formidable challenge to mechanistic understanding. Here, we reconstituted the complete human IFT-A complex and obtained its structure using cryo-EM. Combined with AlphaFold prediction and genome-editing studies, our results illuminate how IFT-A polymerizes, interacts with IFT-B, and uses an array of beta-propeller and TPR domains to create "carriages" of the IFT train that engage TULP adaptor proteins. We show that IFT-AâTULP carriages are essential for cilia localization of diverse membrane proteins, as well as ICK-the key kinase regulating IFT train turnaround. These data establish a structural link between IFT-A's distinct functions, provide a blueprint for IFT-A in the train, and shed light on how IFT evolved from a proto-coatomer ancestor.
-Authors:
+IFT-A structure reveals carriages for membrane protein transport into cilia.,Hesketh SJ, Mukhopadhyay AG, Nakamura D, Toropova K, Roberts AJ Cell. 2022 Nov 30:S0092-8674(22)01422-2. doi: 10.1016/j.cell.2022.11.010. PMID:36462505<ref>PMID:36462505</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 8bbe" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Hesketh SJ]]
+[[Category: Mukhopadhyay AG]]
+[[Category: Nakamura D]]
+[[Category: Roberts AJ]]
+[[Category: Toropova K]]

8bbe

From Proteopedia

Revision as of 09:27, 21 December 2022

Structure of the IFT-A complex; IFT-A2 module

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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