دورية أكاديمية

Cooperation between tropomyosin and α-actinin inhibits fimbrin association with actin filament networks in fission yeast.

التفاصيل البيبلوغرافية
العنوان: Cooperation between tropomyosin and α-actinin inhibits fimbrin association with actin filament networks in fission yeast.
المؤلفون: Christensen JR; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States., Homa KE; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States., Morganthaler AN; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States., Brown RR; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States., Suarez C; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States., Harker AJ; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States., O'Connell ME; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States., Kovar DR; Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States.; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States.
المصدر: ELife [Elife] 2019 Jun 10; Vol. 8. Date of Electronic Publication: 2019 Jun 10.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Actin Cytoskeleton/*metabolism , Actinin/*metabolism , Membrane Glycoproteins/*metabolism , Microfilament Proteins/*metabolism , Schizosaccharomyces/*metabolism , Schizosaccharomyces pombe Proteins/*metabolism , Tropomyosin/*metabolism, Actin Depolymerizing Factors/genetics ; Actin Depolymerizing Factors/metabolism ; Actinin/genetics ; Actins/genetics ; Actins/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Membrane Glycoproteins/genetics ; Microfilament Proteins/genetics ; Microscopy, Fluorescence/methods ; Protein Binding ; Schizosaccharomyces/genetics ; Schizosaccharomyces pombe Proteins/genetics ; Time-Lapse Imaging/methods ; Tropomyosin/genetics
مستخلص: We previously discovered that competition between fission yeast actin binding proteins (ABPs) for binding F-actin facilitates their sorting to different cellular networks. Specifically, competition between endocytic actin patch ABPs fimbrin Fim1 and cofilin Adf1 enhances their activities, and prevents tropomyosin Cdc8's association with actin patches. However, these interactions do not explain how Fim1 is prevented from associating strongly with other F-actin networks such as the contractile ring. Here, we identified α-actinin Ain1, a contractile ring ABP, as another Fim1 competitor. Fim1 competes with Ain1 for association with F-actin, which is dependent upon their F-actin residence time. While Fim1 outcompetes both Ain1 and Cdc8 individually, Cdc8 enhances the F-actin bundling activity of Ain1, allowing Ain1 to generate F-actin bundles that Cdc8 can bind in the presence of Fim1. Therefore, the combination of contractile ring ABPs Ain1 and Cdc8 is capable of inhibiting Fim1's association with F-actin networks.
Competing Interests: JC, KH, AM, RB, CS, AH, MO, DK No competing interests declared
(© 2019, Christensen et al.)
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معلومات مُعتمدة: RSG-11-126-01-CSM International American Cancer Society; T32 GM0071832 United States NH NIH HHS; R01 GM079265 United States GM NIGMS NIH HHS; R01 GM071832 United States GM NIGMS NIH HHS; R25 GM109439 United States GM NIGMS NIH HHS; Graduate Research Fellowship DGE-1746045 International National Science Foundation; R01 GM079265 United States NH NIH HHS; IMSD R25GM109439 United States NH NIH HHS; Graduate Research Fellowship DGE-1144082 International National Science Foundation
فهرسة مساهمة: Keywords: Ain1; Cdc8; S. pombe; actin patch; cell biology; contractile ring; cytokinesis; endocytosis
المشرفين على المادة: 0 (Actin Depolymerizing Factors)
0 (Actins)
0 (Adf1 protein, S pombe)
0 (Cdc8 protein, S pombe)
0 (Cell Cycle Proteins)
0 (Membrane Glycoproteins)
0 (Microfilament Proteins)
0 (Schizosaccharomyces pombe Proteins)
0 (Tropomyosin)
0 (plastin)
11003-00-2 (Actinin)
147336-22-9 (Green Fluorescent Proteins)
تواريخ الأحداث: Date Created: 20190611 Date Completed: 20200302 Latest Revision: 20200309
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC6557641
DOI: 10.7554/eLife.47279
PMID: 31180322
قاعدة البيانات: MEDLINE