دورية أكاديمية
Arp2/3 complex- and formin-mediated actin cytoskeleton networks facilitate actin binding protein sorting in fission yeast.
العنوان: | Arp2/3 complex- and formin-mediated actin cytoskeleton networks facilitate actin binding protein sorting in fission yeast. |
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المؤلفون: | Homa KE; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL, United States., Hocky GM; Department of Chemistry, New York University, New York, NY, United States., Suarez C; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL, United States., Kovar DR; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL, United States; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, United States. Electronic address: drkovar@uchicago.edu. |
المصدر: | European journal of cell biology [Eur J Cell Biol] 2024 Jun; Vol. 103 (2), pp. 151404. Date of Electronic Publication: 2024 Mar 16. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: Elsevier Country of Publication: Germany NLM ID: 7906240 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1618-1298 (Electronic) Linking ISSN: 01719335 NLM ISO Abbreviation: Eur J Cell Biol Subsets: MEDLINE |
أسماء مطبوعة: | Publication: Jena, Germany : Elsevier Original Publication: Stuttgart : Wissenschaftliche Verlagsgesellschaft, <1979-1997> |
مواضيع طبية MeSH: | Schizosaccharomyces*/metabolism , Schizosaccharomyces pombe Proteins*/metabolism , Schizosaccharomyces pombe Proteins*/genetics , Actin-Related Protein 2-3 Complex*/metabolism , Actin Cytoskeleton*/metabolism , Microfilament Proteins*/metabolism , Microfilament Proteins*/genetics, Cell Cycle Proteins/metabolism ; Cell Cycle Proteins/genetics ; Actins/metabolism ; Protein Transport ; Cytoskeletal Proteins ; Membrane Glycoproteins |
مستخلص: | While it is well-established that F-actin networks with specific organizations and dynamics are tightly regulated by distinct sets of associated actin-binding proteins (ABPs), how ABPs self-sort to particular F-actin networks remains largely unclear. We report that actin assembly factors Arp2/3 complex and formin Cdc12 tune the association of ABPs fimbrin Fim1 and tropomyosin Cdc8 to different F-actin networks in fission yeast. Genetic and pharmacological disruption of F-actin networks revealed that Fim1 is preferentially directed to Arp2/3-complex mediated actin patches, whereas Cdc8 is preferentially targeted to formin Cdc12-mediated filaments in the contractile ring. To investigate the role of Arp2/3 complex- and formin Cdc12-mediated actin assembly, we used four-color TIRF microscopy to observe the in vitro reconstitution of ABP sorting with purified proteins. Fim1 or Cdc8 alone bind similarly well to filaments assembled by either assembly factor. However, in 'competition' reactions containing both actin assembly factors and both ABPs, ∼2.0-fold more Fim1 and ∼3.5-fold more Cdc8 accumulates on Arp2/3 complex branch points and formin Cdc12-assembled actin filaments, respectively. These findings indicate that F-actin assembly factors Arp2/3 complex and formin Cdc12 help facilitate the recruitment of specific ABPs, thereby tuning ABP sorting and subsequently establishing the identity of F-actin networks in fission yeast. Competing Interests: Declaration of Competing Interest None. (Copyright © 2024 The Authors. Published by Elsevier GmbH.. All rights reserved.) |
References: | Science. 2005 Oct 14;310(5746):310-4. (PMID: 16224022) Proc Natl Acad Sci U S A. 2020 Oct 13;117(41):25532-25542. (PMID: 32989126) J Biol Chem. 2009 Jan 23;284(4):2088-97. (PMID: 19028693) Curr Opin Cell Biol. 2021 Feb;68:72-80. (PMID: 33160108) PLoS Biol. 2019 Jun 10;17(6):e3000317. (PMID: 31181075) Cell Rep. 2017 Dec 5;21(10):2714-2723. (PMID: 29212020) Nat Rev Mol Cell Biol. 2016 Dec;17(12):799-810. (PMID: 27625321) J Biol Chem. 2011 Jul 29;286(30):26964-77. (PMID: 21642440) Proc Natl Acad Sci U S A. 2012 Oct 16;109(42):16923-7. (PMID: 23027950) Curr Biol. 2001 Aug 21;11(16):1300-4. (PMID: 11525747) J Mol Biol. 1971 Nov 28;62(1):251-65. (PMID: 4945533) Nature. 1999 Oct 7;401(6753):613-6. (PMID: 10524632) J Biol Chem. 1971 Aug 10;246(15):4866-71. (PMID: 4254541) J Cell Sci. 2007 May 1;120(Pt 9):1635-45. (PMID: 17452625) J Cell Biol. 1997 Aug 25;138(4):771-81. (PMID: 9265645) J Cell Biol. 2023 Apr 3;222(4):. (PMID: 36729023) Mol Biol Cell. 2001 Apr;12(4):1061-77. (PMID: 11294907) Trends Cell Biol. 2011 Mar;21(3):177-87. (PMID: 21145239) Dev Cell. 2020 Nov 23;55(4):468-482.e7. (PMID: 33058779) Dev Cell. 2015 Jan 12;32(1):43-53. (PMID: 25543282) J Cell Biol. 2005 Aug 15;170(4):637-48. (PMID: 16087707) Curr Biol. 2010 Aug 24;20(16):1415-22. (PMID: 20705466) Curr Biol. 2016 Dec 5;26(23):3230-3237. (PMID: 27866892) Cytoskeleton (Hoboken). 2021 Jun;78(6):303-311. (PMID: 34028199) Nature. 2009 Aug 20;460(7258):1031-4. (PMID: 19648907) Curr Biol. 2014 Jul 7;24(13):1525-30. (PMID: 24954052) Biophysics (Nagoya-shi). 2012 May 31;8:95-102. (PMID: 27493525) Curr Biol. 2010 Nov 9;20(21):1890-9. (PMID: 21035341) Curr Biol. 2019 Oct 7;29(19):3165-3176.e6. (PMID: 31495586) Nat Commun. 2017 Sep 21;8(1):655. (PMID: 28935896) J Cell Biol. 1993 Feb;120(4):923-34. (PMID: 8432732) Elife. 2017 Mar 10;6:. (PMID: 28282023) Methods Mol Biol. 2016;1369:151-79. (PMID: 26519312) Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4908-13. (PMID: 10220392) Curr Biol. 2016 Oct 24;26(20):2697-2706. (PMID: 27666967) Mol Biol Cell. 2001 Nov;12(11):3515-26. (PMID: 11694585) Curr Biol. 2011 Jul 26;21(14):R560-9. (PMID: 21783039) J Biol Chem. 1995 May 12;270(19):11437-44. (PMID: 7744781) Nat Commun. 2016 Apr 12;7:11265. (PMID: 27068241) Curr Biol. 2015 Jun 15;25(12):1573-82. (PMID: 26028436) Cold Spring Harb Perspect Biol. 2016 Aug 01;8(8):. (PMID: 26988969) Nat Commun. 2017 Sep 26;8(1):703. (PMID: 28951543) Mol Cell. 2005 Apr 29;18(3):273-81. (PMID: 15866170) Annu Rev Cell Dev Biol. 2020 Oct 6;36:35-60. (PMID: 33021819) Curr Biol. 2010 Aug 24;20(16):1423-31. (PMID: 20705471) Elife. 2019 Jun 10;8:. (PMID: 31180322) Mol Biol Cell. 2010 Aug 15;21(16):2894-904. (PMID: 20587778) Biophys J. 2006 Oct 1;91(7):2564-72. (PMID: 16829561) Curr Biol. 2014 Mar 3;24(5):579-85. (PMID: 24560576) Biophys J. 2016 May 24;110(10):2138-46. (PMID: 27224479) PLoS One. 2012;7(6):e39676. (PMID: 22737252) Nat Rev Mol Cell Biol. 2008 Mar;9(3):255-62. (PMID: 18292780) J Cell Biol. 2001 Oct 15;155(2):181-5. (PMID: 11604416) J Cell Biol. 1999 Sep 20;146(6):1319-32. (PMID: 10491394) J Cell Sci. 2022 Sep 15;135(18):. (PMID: 36148799) Proc Natl Acad Sci U S A. 2014 Mar 18;111(11):4121-6. (PMID: 24591594) |
معلومات مُعتمدة: | R01 GM071832 United States GM NIGMS NIH HHS; R01 GM079265 United States GM NIGMS NIH HHS; R35 GM138312 United States GM NIGMS NIH HHS; T32 GM007183 United States GM NIGMS NIH HHS |
فهرسة مساهمة: | Keywords: Actin cytoskeleton; Actin-binding proteins; Arp2/3 complex; Fimbrin; Formin; Tropomyosin |
المشرفين على المادة: | 0 (Schizosaccharomyces pombe Proteins) 0 (Actin-Related Protein 2-3 Complex) 0 (Microfilament Proteins) 0 (Cdc12 protein, S pombe) 0 (Cell Cycle Proteins) 0 (Cdc8 protein, S pombe) 0 (Actins) 0 (plastin) 0 (Cytoskeletal Proteins) 0 (Membrane Glycoproteins) |
تواريخ الأحداث: | Date Created: 20240317 Date Completed: 20240627 Latest Revision: 20240702 |
رمز التحديث: | 20240703 |
مُعرف محوري في PubMed: | PMC11211059 |
DOI: | 10.1016/j.ejcb.2024.151404 |
PMID: | 38493594 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1618-1298 |
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DOI: | 10.1016/j.ejcb.2024.151404 |