|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of the mouse cavin1 HR1 domain== | | ==Crystal structure of the mouse cavin1 HR1 domain== |
| - | <StructureSection load='4qkv' size='340' side='right' caption='[[4qkv]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4qkv' size='340' side='right'caption='[[4qkv]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qkv]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QKV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qkv]] is a 3 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=4QKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QKV FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qkw|4qkw]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkv OCA], [http://pdbe.org/4qkv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qkv RCSB], [http://www.ebi.ac.uk/pdbsum/4qkv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkv ProSAT]</span></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=4qkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkv OCA], [https://pdbe.org/4qkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qkv RCSB], [https://www.ebi.ac.uk/pdbsum/4qkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PTRF_MOUSE PTRF_MOUSE]] Plays an important role in caveolae formation and organization. Required for the sequestration of mobile caveolin into immobile caveolae. Termination of transcription by RNA polymerase I involves pausing of transcription by TTF1, and the dissociation of the transcription complex, releasing pre-rRNA and RNA polymerase I from the template. PTRF is required for dissociation of the ternary transcription complex.<ref>PMID:11139612</ref> <ref>PMID:18056712</ref> <ref>PMID:18191225</ref> <ref>PMID:18840361</ref> <ref>PMID:9582279</ref> | + | [https://www.uniprot.org/uniprot/CAVN1_MOUSE CAVN1_MOUSE] Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18191225, PubMed:18840361, PubMed:18056712, PubMed:30188967). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1) (PubMed:19546242). Essential for normal oligomerization of CAV1 (PubMed:23652019). Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop (PubMed:27528195). Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (PubMed:9582279, PubMed:11139612). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (PubMed:30188967).<ref>PMID:11139612</ref> <ref>PMID:18056712</ref> <ref>PMID:18191225</ref> <ref>PMID:18840361</ref> <ref>PMID:19546242</ref> <ref>PMID:23652019</ref> <ref>PMID:27528195</ref> <ref>PMID:30188967</ref> <ref>PMID:9582279</ref> |
| - | <div style="background-color:#fffaf0;"> | + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Caveolae are cell-surface membrane invaginations that play critical roles in cellular processes including signaling and membrane homeostasis. The cavin proteins, in cooperation with caveolins, are essential for caveola formation. Here we show that a minimal N-terminal domain of the cavins, termed HR1, is required and sufficient for their homo- and hetero-oligomerization. Crystal structures of the mouse cavin1 and zebrafish cavin4a HR1 domains reveal highly conserved trimeric coiled-coil architectures, with intersubunit interactions that determine the specificity of cavin-cavin interactions. The HR1 domain contains a basic surface patch that interacts with polyphosphoinositides and coordinates with additional membrane-binding sites within the cavin C terminus to facilitate membrane association and remodeling. Electron microscopy of purified cavins reveals the existence of large assemblies, composed of a repeating rod-like structural element, and we propose that these structures polymerize through membrane-coupled interactions to form the unique striations observed on the surface of caveolae in vivo.
| + | |
| - | | + | |
| - | Structural insights into the organization of the cavin membrane coat complex.,Kovtun O, Tillu VA, Jung W, Leneva N, Ariotti N, Chaudhary N, Mandyam RA, Ferguson C, Morgan GP, Johnston WA, Harrop SJ, Alexandrov K, Parton RG, Collins BM Dev Cell. 2014 Nov 24;31(4):405-19. doi: 10.1016/j.devcel.2014.10.002. Epub 2014 , Nov 13. PMID:25453557<ref>PMID:25453557</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 4qkv" style="background-color:#fffaf0;"></div> | + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Collins, B M]] | + | [[Category: Large Structures]] |
| - | [[Category: Kovtun, O]] | + | [[Category: Mus musculus]] |
| - | [[Category: Parton, R G]] | + | [[Category: Collins BM]] |
| - | [[Category: Tillu, V]] | + | [[Category: Kovtun O]] |
| - | [[Category: Coiled-coil]] | + | [[Category: Parton RG]] |
| - | [[Category: Plasma membrane]] | + | [[Category: Tillu V]] |
| - | [[Category: Signalling]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
CAVN1_MOUSE Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18191225, PubMed:18840361, PubMed:18056712, PubMed:30188967). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1) (PubMed:19546242). Essential for normal oligomerization of CAV1 (PubMed:23652019). Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop (PubMed:27528195). Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (PubMed:9582279, PubMed:11139612). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (PubMed:30188967).[1] [2] [3] [4] [5] [6] [7] [8] [9]
References
- ↑ Jansa P, Burek C, Sander EE, Grummt I. The transcript release factor PTRF augments ribosomal gene transcription by facilitating reinitiation of RNA polymerase I. Nucleic Acids Res. 2001 Jan 15;29(2):423-9. PMID:11139612
- ↑ Liu L, Pilch PF. A critical role of cavin (polymerase I and transcript release factor) in caveolae formation and organization. J Biol Chem. 2008 Feb 15;283(7):4314-22. Epub 2007 Dec 3. PMID:18056712 doi:http://dx.doi.org/10.1074/jbc.M707890200
- ↑ Hill MM, Bastiani M, Luetterforst R, Kirkham M, Kirkham A, Nixon SJ, Walser P, Abankwa D, Oorschot VM, Martin S, Hancock JF, Parton RG. PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation and function. Cell. 2008 Jan 11;132(1):113-24. PMID:18191225 doi:http://dx.doi.org/S0092-8674(07)01546-2
- ↑ Liu L, Brown D, McKee M, Lebrasseur NK, Yang D, Albrecht KH, Ravid K, Pilch PF. Deletion of Cavin/PTRF causes global loss of caveolae, dyslipidemia, and glucose intolerance. Cell Metab. 2008 Oct;8(4):310-7. doi: 10.1016/j.cmet.2008.07.008. PMID:18840361 doi:http://dx.doi.org/10.1016/j.cmet.2008.07.008
- ↑ Bastiani M, Liu L, Hill MM, Jedrychowski MP, Nixon SJ, Lo HP, Abankwa D, Luetterforst R, Fernandez-Rojo M, Breen MR, Gygi SP, Vinten J, Walser PJ, North KN, Hancock JF, Pilch PF, Parton RG. MURC/Cavin-4 and cavin family members form tissue-specific caveolar complexes. J Cell Biol. 2009 Jun 29;185(7):1259-73. PMID:19546242 doi:10.1083/jcb.200903053
- ↑ Hansen CG, Shvets E, Howard G, Riento K, Nichols BJ. Deletion of cavin genes reveals tissue-specific mechanisms for morphogenesis of endothelial caveolae. Nat Commun. 2013;4:1831. PMID:23652019 doi:10.1038/ncomms2808
- ↑ Liu L, Pilch PF. PTRF/Cavin-1 promotes efficient ribosomal RNA transcription in response to metabolic challenges. Elife. 2016 Aug 16;5:e17508. PMID:27528195 doi:10.7554/eLife.17508
- ↑ Wei Z, Liu T, Lei J, Wu Y, Wang S, Liao K. Fam198a, a member of secreted kinase, secrets through caveolae biogenesis pathway. Acta Biochim Biophys Sin (Shanghai). 2018 Oct 1;50(10):968-975. PMID:30188967 doi:10.1093/abbs/gmy105
- ↑ Jansa P, Mason SW, Hoffmann-Rohrer U, Grummt I. Cloning and functional characterization of PTRF, a novel protein which induces dissociation of paused ternary transcription complexes. EMBO J. 1998 May 15;17(10):2855-64. PMID:9582279 doi:http://dx.doi.org/10.1093/emboj/17.10.2855
|
