5hmo

From Proteopedia

(Difference between revisions)

Revision as of 08:23, 27 May 2020

myosin X motor activity

Structural highlights

5hmo is a 2 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	MYO10 (BOVIN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYO10_BOVIN] In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Publication Abstract from PubMed

Myosin X has features not found in other myosins. Its structure must underlie its unique ability to generate filopodia, which are essential for neuritogenesis, wound healing, cancer metastasis and some pathogenic infections. By determining high-resolution structures of key components of this motor, and characterizing the in vitro behaviour of the native dimer, we identify the features that explain the myosin X dimer behaviour. Single-molecule studies demonstrate that a native myosin X dimer moves on actin bundles with higher velocities and takes larger steps than on single actin filaments. The largest steps on actin bundles are larger than previously reported for artificially dimerized myosin X constructs or any other myosin. Our model and kinetic data explain why these large steps and high velocities can only occur on bundled filaments. Thus, myosin X functions as an antiparallel dimer in cells with a unique geometry optimized for movement on actin bundles.

The myosin X motor is optimized for movement on actin bundles.,Ropars V, Yang Z, Isabet T, Blanc F, Zhou K, Lin T, Liu X, Hissier P, Samazan F, Amigues B, Yang ED, Park H, Pylypenko O, Cecchini M, Sindelar CV, Sweeney HL, Houdusse A Nat Commun. 2016 Sep 1;7:12456. doi: 10.1038/ncomms12456. PMID:27580874^[10]

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

References

↑ Homma K, Saito J, Ikebe R, Ikebe M. Motor function and regulation of myosin X. J Biol Chem. 2001 Sep 7;276(36):34348-54. Epub 2001 Jul 16. PMID:11457842 doi:http://dx.doi.org/10.1074/jbc.M104785200
↑ Zhang H, Berg JS, Li Z, Wang Y, Lang P, Sousa AD, Bhaskar A, Cheney RE, Stromblad S. Myosin-X provides a motor-based link between integrins and the cytoskeleton. Nat Cell Biol. 2004 Jun;6(6):523-31. Epub 2004 May 23. PMID:15156152 doi:http://dx.doi.org/10.1038/ncb1136
↑ Kovacs M, Wang F, Sellers JR. Mechanism of action of myosin X, a membrane-associated molecular motor. J Biol Chem. 2005 Apr 15;280(15):15071-83. Epub 2005 Feb 10. PMID:15705568 doi:http://dx.doi.org/10.1074/jbc.M500616200
↑ Bohil AB, Robertson BW, Cheney RE. Myosin-X is a molecular motor that functions in filopodia formation. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12411-6. Epub 2006 Aug 7. PMID:16894163 doi:10.1073/pnas.0602443103
↑ McMichael BK, Cheney RE, Lee BS. Myosin X regulates sealing zone patterning in osteoclasts through linkage of podosomes and microtubules. J Biol Chem. 2010 Mar 26;285(13):9506-15. doi: 10.1074/jbc.M109.017269. Epub 2010, Jan 17. PMID:20081229 doi:http://dx.doi.org/10.1074/jbc.M109.017269
↑ Sun Y, Sato O, Ruhnow F, Arsenault ME, Ikebe M, Goldman YE. Single-molecule stepping and structural dynamics of myosin X. Nat Struct Mol Biol. 2010 Apr;17(4):485-91. doi: 10.1038/nsmb.1785. Epub 2010 Apr, 4. PMID:20364131 doi:http://dx.doi.org/10.1038/nsmb.1785
↑ Watanabe TM, Tokuo H, Gonda K, Higuchi H, Ikebe M. Myosin-X induces filopodia by multiple elongation mechanism. J Biol Chem. 2010 Jun 18;285(25):19605-14. doi: 10.1074/jbc.M109.093864. Epub, 2010 Apr 13. PMID:20392702 doi:http://dx.doi.org/10.1074/jbc.M109.093864
↑ Plantard L, Arjonen A, Lock JG, Nurani G, Ivaska J, Stromblad S. PtdIns(3,4,5)P(3) is a regulator of myosin-X localization and filopodia formation. J Cell Sci. 2010 Oct 15;123(Pt 20):3525-34. doi: 10.1242/jcs.069609. PMID:20930142 doi:http://dx.doi.org/10.1242/jcs.069609
↑ Umeki N, Jung HS, Sakai T, Sato O, Ikebe R, Ikebe M. Phospholipid-dependent regulation of the motor activity of myosin X. Nat Struct Mol Biol. 2011 Jun 12;18(7):783-8. doi: 10.1038/nsmb.2065. PMID:21666676 doi:http://dx.doi.org/10.1038/nsmb.2065
↑ Ropars V, Yang Z, Isabet T, Blanc F, Zhou K, Lin T, Liu X, Hissier P, Samazan F, Amigues B, Yang ED, Park H, Pylypenko O, Cecchini M, Sindelar CV, Sweeney HL, Houdusse A. The myosin X motor is optimized for movement on actin bundles. Nat Commun. 2016 Sep 1;7:12456. doi: 10.1038/ncomms12456. PMID:27580874 doi:http://dx.doi.org/10.1038/ncomms12456

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5hmo"

@@ Line 1: / Line 1: @@
 ==myosin X motor activity==
-<StructureSection load='5hmo' size='340' side='right' caption='[[5hmo]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
+<StructureSection load='5hmo' size='340' side='right'caption='[[5hmo]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hmo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HMO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5hmo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HMO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HMO FirstGlance]. <br>
-</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=5hmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hmo OCA], [http://pdbe.org/5hmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hmo RCSB], [http://www.ebi.ac.uk/pdbsum/5hmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hmo ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hmo OCA], [http://pdbe.org/5hmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hmo RCSB], [http://www.ebi.ac.uk/pdbsum/5hmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hmo ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 5hmo" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Myosin 3D Structures|Myosin 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Bovin]]
+[[Category: Large Structures]]
 [[Category: Blanc, F]]
 [[Category: Houdusse, A]]

5hmo

From Proteopedia

Revision as of 08:23, 27 May 2020

myosin X motor activity

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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