Show simple item record

dc.contributor.authorLuna, Elizabeth J.
dc.contributor.authorFowler, V. M.
dc.contributor.authorSwanson, J.
dc.contributor.authorBranton, D.
dc.contributor.authorTaylor, D. L.
dc.date2022-08-11T08:11:04.000
dc.date.accessioned2022-08-23T17:31:33Z
dc.date.available2022-08-23T17:31:33Z
dc.date.issued1981-02-01
dc.date.submitted2007-11-13
dc.identifier.citation<p>J Cell Biol. 1981 Feb;88(2):396-409. <a href="http://dx.doi.org/10.1083/jcb.88.2.396 ">Link to article on publisher's website</a></p>
dc.identifier.issn0021-9525 (Print)
dc.identifier.doi10.1083/jcb.88.2.396
dc.identifier.pmid6894148
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50760
dc.description.abstractDictyostelium discoideum plasma membranes isolated by each of three procedures bind F-actin. The interactions between these membranes and actin are examined by a novel application of falling ball viscometry. Treating the membranes as multivalent actin-binding particles analogous to divalent actin-gelation factors, we observe large increases in viscosity (actin cross-linking) when membranes of depleted actin and myosin are incubated with rabbit skeletal muscle F-actin. Pre-extraction of peripheral membrane proteins with chaotropes or the inclusion of Triton X-100 during the assay does not appreciably diminish this actin cross-linking activity. Lipid vesicles, heat-denatured membranes, proteolyzed membranes, or membranes containing endogenous actin show minimal actin cross-linking activity. Heat-denatured, but not proteolyzed, membranes regain activity when assayed in the presence of Triton X-100. Thus, integral membrane proteins appear to be responsible for some or all of the actin cross-linking activity of D. discoideum membranes. In the absence of MgATP, Triton X-100 extraction of isolated D. discoideum membranes results in a Triton-insoluble residue composed of actin, myosin, and associated membrane proteins. The inclusion of MgATP before and during Triton extraction greatly diminishes the amount of protein in the Triton-insoluble residue without appreciably altering its composition. Our results suggest the existence of a protein complex stabilized by actin and/or myosin (membrane cytoskeleton) associated with the D. discoideum plasma membrane.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6894148&dopt=Abstract">Link to article in PubMed</a></p>
dc.rightsPublisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.subjectActins
dc.subjectCell Membrane
dc.subjectDictyostelium
dc.subjectMembrane Lipids
dc.subjectMembrane Proteins
dc.subjectPolyethylene Glycols
dc.subjectViscosity
dc.subjectCell Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleA membrane cytoskeleton from Dictyostelium discoideum. I. Identification and partial characterization of an actin-binding activity
dc.typeJournal Article
dc.source.journaltitleThe Journal of cell biology
dc.source.volume88
dc.source.issue2
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1287&amp;context=wfc_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/wfc_pp/288
dc.identifier.contextkey392372
refterms.dateFOA2022-08-23T17:31:33Z
html.description.abstract<p>Dictyostelium discoideum plasma membranes isolated by each of three procedures bind F-actin. The interactions between these membranes and actin are examined by a novel application of falling ball viscometry. Treating the membranes as multivalent actin-binding particles analogous to divalent actin-gelation factors, we observe large increases in viscosity (actin cross-linking) when membranes of depleted actin and myosin are incubated with rabbit skeletal muscle F-actin. Pre-extraction of peripheral membrane proteins with chaotropes or the inclusion of Triton X-100 during the assay does not appreciably diminish this actin cross-linking activity. Lipid vesicles, heat-denatured membranes, proteolyzed membranes, or membranes containing endogenous actin show minimal actin cross-linking activity. Heat-denatured, but not proteolyzed, membranes regain activity when assayed in the presence of Triton X-100. Thus, integral membrane proteins appear to be responsible for some or all of the actin cross-linking activity of D. discoideum membranes. In the absence of MgATP, Triton X-100 extraction of isolated D. discoideum membranes results in a Triton-insoluble residue composed of actin, myosin, and associated membrane proteins. The inclusion of MgATP before and during Triton extraction greatly diminishes the amount of protein in the Triton-insoluble residue without appreciably altering its composition. Our results suggest the existence of a protein complex stabilized by actin and/or myosin (membrane cytoskeleton) associated with the D. discoideum plasma membrane.</p>
dc.identifier.submissionpathwfc_pp/288
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages396-409


Files in this item

Thumbnail
Name:
6894148.pdf
Size:
1.846Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record

Publisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.
Except where otherwise noted, this item's license is described as Publisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.