Identification of an actin-binding protein from Dictyostelium as elongation factor 1a

Fan Yang, Mark Demma, Vivien Warren, Suranganie Dharmawardhane, John S. Condeelis

Research output: Contribution to journalArticle

275 Citations (Scopus)

Abstract

INDIRECT evidence has implicated an interaction between the cytoskeleton and the protein synthetic machinery1-8. Two recent reports have linked the elongation factor 1a (EF-1a) which is involved in protein synthesis, with the microtubular cytoskeleton7-8. In situ hybridization has, however, revealed that the messages for certain cytoskeletal proteins are preferentially associated with actin filaments6. ABP-50 is an abundant actin filament bundling protein of native relative molecular mass 50,000 (50K)9 isolated from Dictyostelium discoideum. Immunofluorescence studies show that ABP-50 is present in filopodia and other cortical regions that contain actin filament bundles9,10. In addition, ABP-50 binds to monomeric actin in the cytosol of unstimulated cells and the association of ABP-50 with the actin cytoskeleton is regulated during chemotaxis10. Through complementary DNA sequencing and subsequent functional analysis, we have identified ABP-50 as D. discoideum EF-1a. The ability of EF-1a to bind reversibly to the actin cytoskeleton upon stimulation could provide a mechanism for spatially and temporally regulated protein synthesis in eukaryotic cells.

Original languageEnglish (US)
Pages (from-to)494-496
Number of pages3
JournalNature
Volume347
Issue number6292
StatePublished - Oct 4 1990

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Peptide Elongation Factors
Microfilament Proteins
Dictyostelium
Actin Cytoskeleton
Actins
Proteins
Pseudopodia
Cytoskeletal Proteins
Eukaryotic Cells
Cytoskeleton
DNA Sequence Analysis
Cytosol
In Situ Hybridization
Fluorescent Antibody Technique
Complementary DNA

ASJC Scopus subject areas

  • General

Cite this

Yang, F., Demma, M., Warren, V., Dharmawardhane, S., & Condeelis, J. S. (1990). Identification of an actin-binding protein from Dictyostelium as elongation factor 1a. Nature, 347(6292), 494-496.

Identification of an actin-binding protein from Dictyostelium as elongation factor 1a. / Yang, Fan; Demma, Mark; Warren, Vivien; Dharmawardhane, Suranganie; Condeelis, John S.

In: Nature, Vol. 347, No. 6292, 04.10.1990, p. 494-496.

Research output: Contribution to journalArticle

Yang, F, Demma, M, Warren, V, Dharmawardhane, S & Condeelis, JS 1990, 'Identification of an actin-binding protein from Dictyostelium as elongation factor 1a', Nature, vol. 347, no. 6292, pp. 494-496.
Yang F, Demma M, Warren V, Dharmawardhane S, Condeelis JS. Identification of an actin-binding protein from Dictyostelium as elongation factor 1a. Nature. 1990 Oct 4;347(6292):494-496.
Yang, Fan ; Demma, Mark ; Warren, Vivien ; Dharmawardhane, Suranganie ; Condeelis, John S. / Identification of an actin-binding protein from Dictyostelium as elongation factor 1a. In: Nature. 1990 ; Vol. 347, No. 6292. pp. 494-496.
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abstract = "INDIRECT evidence has implicated an interaction between the cytoskeleton and the protein synthetic machinery1-8. Two recent reports have linked the elongation factor 1a (EF-1a) which is involved in protein synthesis, with the microtubular cytoskeleton7-8. In situ hybridization has, however, revealed that the messages for certain cytoskeletal proteins are preferentially associated with actin filaments6. ABP-50 is an abundant actin filament bundling protein of native relative molecular mass 50,000 (50K)9 isolated from Dictyostelium discoideum. Immunofluorescence studies show that ABP-50 is present in filopodia and other cortical regions that contain actin filament bundles9,10. In addition, ABP-50 binds to monomeric actin in the cytosol of unstimulated cells and the association of ABP-50 with the actin cytoskeleton is regulated during chemotaxis10. Through complementary DNA sequencing and subsequent functional analysis, we have identified ABP-50 as D. discoideum EF-1a. The ability of EF-1a to bind reversibly to the actin cytoskeleton upon stimulation could provide a mechanism for spatially and temporally regulated protein synthesis in eukaryotic cells.",
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N2 - INDIRECT evidence has implicated an interaction between the cytoskeleton and the protein synthetic machinery1-8. Two recent reports have linked the elongation factor 1a (EF-1a) which is involved in protein synthesis, with the microtubular cytoskeleton7-8. In situ hybridization has, however, revealed that the messages for certain cytoskeletal proteins are preferentially associated with actin filaments6. ABP-50 is an abundant actin filament bundling protein of native relative molecular mass 50,000 (50K)9 isolated from Dictyostelium discoideum. Immunofluorescence studies show that ABP-50 is present in filopodia and other cortical regions that contain actin filament bundles9,10. In addition, ABP-50 binds to monomeric actin in the cytosol of unstimulated cells and the association of ABP-50 with the actin cytoskeleton is regulated during chemotaxis10. Through complementary DNA sequencing and subsequent functional analysis, we have identified ABP-50 as D. discoideum EF-1a. The ability of EF-1a to bind reversibly to the actin cytoskeleton upon stimulation could provide a mechanism for spatially and temporally regulated protein synthesis in eukaryotic cells.

AB - INDIRECT evidence has implicated an interaction between the cytoskeleton and the protein synthetic machinery1-8. Two recent reports have linked the elongation factor 1a (EF-1a) which is involved in protein synthesis, with the microtubular cytoskeleton7-8. In situ hybridization has, however, revealed that the messages for certain cytoskeletal proteins are preferentially associated with actin filaments6. ABP-50 is an abundant actin filament bundling protein of native relative molecular mass 50,000 (50K)9 isolated from Dictyostelium discoideum. Immunofluorescence studies show that ABP-50 is present in filopodia and other cortical regions that contain actin filament bundles9,10. In addition, ABP-50 binds to monomeric actin in the cytosol of unstimulated cells and the association of ABP-50 with the actin cytoskeleton is regulated during chemotaxis10. Through complementary DNA sequencing and subsequent functional analysis, we have identified ABP-50 as D. discoideum EF-1a. The ability of EF-1a to bind reversibly to the actin cytoskeleton upon stimulation could provide a mechanism for spatially and temporally regulated protein synthesis in eukaryotic cells.

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