title: The association of myosin IB with actin waves in dictyostelium requires both the plasma membrane-binding site and actin-binding region in the myosin tail.
abstract: F-actin structures and their distribution are important determinants of the dynamic shapes and functions of eukaryotic cells. Actin waves are F-actin formations that move along the ventral cell membrane driven by actin polymerization. Dictyostelium myosin IB is associated with actin waves but its role in the wave is unknown. Myosin IB is a monomeric, non-filamentous myosin with a globular head that binds to F-actin and has motor activity, and a non-helical tail comprising a basic region, a glycine-proline-glutamine-rich region and an SH3-domain. The basic region binds to acidic phospholipids in the plasma membrane through a short basic-hydrophobic site and the Gly-Pro-Gln region binds F-actin. In the current work we found that both the basic-hydrophobic site in the basic region and the Gly-Pro-Gln region of the tail are required for the association of myosin IB with actin waves. This is the first evidence that the Gly-Pro-Gln region is required for localization of myosin IB to a specific actin structure in situ. The head is not required for myosin IB association with actin waves but binding of the head to F-actin strengthens the association of myosin IB with waves and stabilizes waves. Neither the SH3-domain nor motor activity is required for association of myosin IB with actin waves. We conclude that myosin IB contributes to anchoring actin waves to the plasma membranes by binding of the basic-hydrophobic site to acidic phospholipids in the plasma membrane and binding of the Gly-Pro-Gln region to F-actin in the wave.
authors.affiliation: Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
authors.forename: Hanna
authors.initials: H
authors.lastname: Brzeska
authors.affiliation: Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
authors.forename: Kevin
authors.initials: K
authors.lastname: Pridham
authors.affiliation: Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
authors.forename: Godefroy
authors.initials: G
authors.lastname: Chery
authors.affiliation: Department of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, Minnesota, United States of America.
authors.forename: Margaret A
authors.initials: MA
authors.lastname: Titus
authors.affiliation: Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
authors.forename: Edward D
authors.initials: ED
authors.lastname: Korn
mesh_terms: D000199:Actins / Q000378:metabolism*; D001665:Binding Sites; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism*; D004023:Dictyostelium / Q000166:cytology* / Q000187:drug effects / Q000378:metabolism*; D017353:Gene Deletion; D024461:Myosin Type I / Q000737:chemistry* / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport / Q000187:drug effects; D053778:Thiazolidines / Q000494:pharmacology; D018909:src Homology Domains
chemical_list: D000199:Actins; D053778:Thiazolidines; D024461:Myosin Type I
references.citation: J Cell Biol. 1997 Feb 10;136(3):633-47
references.pmid: 9024693
references.citation: PLoS Biol. 2007 Sep;5(9):e221
references.pmid: 17696648
references.citation: J Biol Chem. 1989 Nov 15;264(32):19340-8
references.pmid: 2530230
references.citation: Mol Biol Cell. 1996 Jul;7(7):1123-36
references.pmid: 8862525
references.citation: Trends Cell Biol. 2010 Jul;20(7):418-26
references.pmid: 20471271
references.citation: J Biol Chem. 2008 Nov 14;283(46):32014-23
references.pmid: 18772133
references.citation: Plasmid. 2009 Mar;61(2):110-8
references.pmid: 19063918
references.citation: J Eukaryot Microbiol. 1994 Nov-Dec;41(6):652-7
references.pmid: 7866390
references.citation: Cell Motil Cytoskeleton. 1995;31(2):87-92
references.pmid: 7553910
references.citation: FEBS Lett. 2004 Nov 5;577(1-2):227-32
references.pmid: 15527790
references.citation: J Biol Chem. 1973 Jul 10;248(13):4691-7
references.pmid: 4268864
references.citation: Cell Adh Migr. 2009 Oct-Dec;3(4):373-82
references.pmid: 19855162
references.citation: Plasmid. 2000 Nov;44(3):231-8
references.pmid: 11078649
references.citation: Nat Methods. 2008 Jul;5(7):605-7
references.pmid: 18536722
references.citation: Exp Cell Res. 2002 Apr 15;275(1):54-66
references.pmid: 11925105
references.citation: J Cell Biol. 1995 Dec;131(5):1205-21
references.pmid: 8522584
references.citation: Phys Rev Lett. 2010 Jun 4;104(22):228102
references.pmid: 20867207
references.citation: J Biol Chem. 2006 Mar 10;281(10):6307-15
references.pmid: 16415352
references.citation: Biochim Biophys Acta. 2001 Mar 15;1525(3):245-61
references.pmid: 11257438
references.citation: PLoS One. 2011;6(11):e26631
references.pmid: 22069459
references.citation: J Cell Biol. 2001 Jun 25;153(7):1479-97
references.pmid: 11425877
references.citation: Nat Protoc. 2007;2(6):1317-24
references.pmid: 17545968
references.citation: Cell Motil Cytoskeleton. 2008 Dec;65(12):923-34
references.pmid: 18814278
references.citation: Methods Cell Biol. 1987;28:9-29
references.pmid: 3298997
references.citation: Phys Rev Lett. 2011 Dec 16;107(25):258103
references.pmid: 22243118
references.citation: J Biol Chem. 2008 Feb 22;283(8):4520-7
references.pmid: 18089562
references.citation: Biochemistry. 1997 Nov 18;36(46):14037-43
references.pmid: 9369475
references.citation: Nat Cell Biol. 2011 Jun 12;13(7):779-89
references.pmid: 21666684
references.citation: Curr Biol. 2004 Jan 6;14(1):1-10
references.pmid: 14711408
references.citation: Biophys J. 2009 Apr 8;96(7):2888-900
references.pmid: 19348770
references.citation: J Biol Chem. 1996 Jul 19;271(29):16983-6
references.pmid: 8707782
references.citation: Proc Natl Acad Sci U S A. 2013 Mar 26;110(13):5016-21
references.pmid: 23479620
references.citation: Annu Rev Biophys. 2010;39:91-110
references.pmid: 20462375
references.citation: BMC Cell Biol. 2011 Oct 07;12:42
references.pmid: 21982379
references.citation: PMC Biophys. 2010 Mar 18;3(1):7
references.pmid: 20298542
references.citation: Curr Biol. 2009 Jun 9;19(11):967-73
references.pmid: 19398338
references.citation: Biophys J. 2012 Sep 19;103(6):1170-8
references.pmid: 22995489
references.citation: Science. 2009 Nov 27;326(5957):1208-12
references.pmid: 19965462
references.citation: Plasmid. 1993 Sep;30(2):150-4
references.pmid: 8234487
references.citation: J Cell Biol. 1990 Jun;110(6):1955-64
references.pmid: 2141028
references.citation: J Cell Biol. 1996 Apr;133(2):305-23
references.pmid: 8609164
references.citation: Phys Rev Lett. 2009 May 15;102(19):198103
references.pmid: 19519000
references.citation: PLoS One. 2013 May 31;8(5):e64272
references.pmid: 23741312
references.citation: Biochemistry. 1994 Mar 1;33(8):2322-8
references.pmid: 8117689
references.citation: Proc Natl Acad Sci U S A. 2001 Jul 31;98(16):9122-7
references.pmid: 11459943
references.citation: J Biol Chem. 1993 Oct 5;268(28):20923-9
references.pmid: 8407927
references.citation: J Biol Chem. 2012 Apr 27;287(18):14923-36
references.pmid: 22367211
references.citation: Biophys J. 2004 Nov;87(5):3493-503
references.pmid: 15347592
references.citation: Annu Rev Physiol. 1991;53:653-81
references.pmid: 2042976
references.citation: J Biol Chem. 2010 Feb 19;285(8):5738-47
references.pmid: 20018884
references.citation: Biochemistry. 1998 Jul 7;37(27):9679-87
references.pmid: 9657680
references.citation: J Cell Sci. 2003 Oct 1;116(Pt 19):3985-99
references.pmid: 12953059
references.citation: J Cell Biol. 1996 Apr;133(2):221-4
references.pmid: 8609156
references.citation: HFSP J. 2009 Dec;3(6):412-27
references.pmid: 20514132
references.citation: FEBS Lett. 2002 Jan 2;510(1-2):5-9
references.pmid: 11755520