title: A requirement for epsin in mitotic membrane and spindle organization.
abstract: Eukaryotic cells possess a sophisticated membrane system to facilitate diverse functions. Whereas much is known about the nature of membrane systems in interphase, the organization and function of the mitotic membrane system are less well understood. In this study, we show that epsin, an endocytic adapter protein, regulates mitotic membrane morphology and spindle integrity in HeLa cells. Using epsin that harbors point mutations in the epsin NH2-terminal homology domain and spindle assembly assays in Xenopus laevis egg extracts, we show that epsin-induced membrane curvature is required for proper spindle morphogenesis, independent of its function in endocytosis during interphase. Although several other membrane-interacting proteins, including clathrin, AP2, autosomal recessive hypercholesterolemia, and GRASP65, are implicated in the regulation of mitosis, whether they participate through regulation of membrane organization is unclear. Our study of epsin provides evidence that mitotic membrane organization influences spindle integrity.
authors.affiliation: Department of Embryology and 2 Howard Hughes Medical Institute, Carnegie Institution of Washington, Baltimore, MD 21218, USA. zliu@ciwemb.edu
authors.forename: Zhonghua
authors.initials: Z
authors.lastname: Liu
authors.forename: Yixian
authors.initials: Y
authors.lastname: Zheng
mesh_terms: D033942:Adaptor Proteins, Vesicular Transport / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D004705:Endocytosis / Q000502:physiology; D006367:HeLa Cells; D006657:Histones / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008938:Mitosis / Q000502:physiology*; D009865:Oocytes / Q000378:metabolism; D017354:Point Mutation; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D008941:Spindle Apparatus / Q000378:metabolism / Q000648:ultrastructure; D014404:Tubulin / Q000235:genetics / Q000378:metabolism; D014982:Xenopus laevis
chemical_list: D033942:Adaptor Proteins, Vesicular Transport; D006657:Histones; D034741:RNA, Small Interfering; D011993:Recombinant Fusion Proteins; D014404:Tubulin; C114154:epsin
references.citation: Curr Biol. 2002 Jul 9;12(13):1112-6
references.pmid: 12121618
references.citation: Nat Cell Biol. 2009 Mar;11(3):247-56
references.pmid: 19198602
references.citation: Cell. 2003 Oct 31;115(3):355-67
references.pmid: 14636562
references.citation: Mol Biol Cell. 2005 Jul;16(7):3211-22
references.pmid: 15888544
references.citation: Mol Biol Cell. 2008 Jul;19(7):2949-61
references.pmid: 18417616
references.citation: Int J Biochem Cell Biol. 2007;39(10):1765-70
references.pmid: 17276129
references.citation: Cell. 1994 Feb 25;76(4):639-50
references.pmid: 8124707
references.citation: Methods Cell Biol. 1991;36:581-605
references.pmid: 1839804
references.citation: Mol Biol Cell. 2001 Jul;12(7):2047-60
references.pmid: 11452002
references.citation: J Biol Chem. 2003 Aug 15;278(33):30597-604
references.pmid: 12775724
references.citation: Proc Natl Acad Sci U S A. 2007 May 8;104(19):7939-44
references.pmid: 17483462
references.citation: Biochim Biophys Acta. 2006 Aug;1761(8):897-912
references.pmid: 16938488
references.citation: Nature. 2005 Apr 28;434(7037):1152-7
references.pmid: 15858577
references.citation: Cell Motil Cytoskeleton. 1993;26(1):19-39
references.pmid: 8106173
references.citation: Mol Biol Cell. 2006 Feb;17(2):990-1005
references.pmid: 16314396
references.citation: Cell Cycle. 2004 Apr;3(4):422-4
references.pmid: 15004522
references.citation: Science. 2006 Mar 31;311(5769):1887-93
references.pmid: 16543417
references.citation: Science. 2001 Feb 9;291(5506):1047-51
references.pmid: 11161217
references.citation: Dev Cell. 2007 Jun;12(6):839-40
references.pmid: 17543853
references.citation: J Biol Chem. 1999 Feb 5;274(6):3257-60
references.pmid: 9920862
references.citation: Dev Cell. 2007 Jun;12(6):917-30
references.pmid: 17543864
references.citation: Mol Biol Cell. 2004 Apr;15(4):1843-52
references.pmid: 14767069
references.citation: Cell Cycle. 2006 Oct;5(20):2345-7
references.pmid: 17102624
references.citation: J Cell Biol. 2009 Mar 9;184(5):677-90
references.pmid: 19255246
references.citation: Science. 2005 Dec 2;310(5753):1499-504
references.pmid: 16322459
references.citation: J Biol Chem. 2003 Aug 1;278(31):28823-30
references.pmid: 12750376
references.citation: J Biol Chem. 2000 Jun 16;275(24):18399-406
references.pmid: 10764745
references.citation: J Cell Biol. 2007 Dec 3;179(5):895-909
references.pmid: 18056408
references.citation: Nature. 2002 Sep 26;419(6905):361-6
references.pmid: 12353027
references.citation: Nature. 2002 Mar 28;416(6879):451-5
references.pmid: 11919637
references.citation: Nature. 2005 Dec 1;438(7068):590-6
references.pmid: 16319878
references.citation: Nat Rev Mol Cell Biol. 2007 Jun;8(6):429-39
references.pmid: 17505521
references.citation: J Cell Biol. 2009 Feb 9;184(3):391-7
references.pmid: 19188490
references.citation: J Biol Chem. 2004 Apr 16;279(16):16657-61
references.pmid: 14985334