{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,4]],"date-time":"2026-02-04T19:43:57Z","timestamp":1770234237428,"version":"3.49.0"},"reference-count":33,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2000,8,1]],"date-time":"2000-08-01T00:00:00Z","timestamp":965088000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2000,8,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Human lymphocyte-specific protein 1 (LSP1) is an F-actin binding protein, which has an acidic N-terminal half and a basic C-terminal half. In the basic C-terminal half, there are amino acid sequences highly homologous to the actin-binding domains of two known F-actin binding proteins: caldesmon and the villin headpieces (CI, CII, VI, VII). However, the exact numbers and locations of the F-actin binding domains within LSP1 are not clearly defined. In this report, we utilized 125I-labeled F-actin ligand blotting and high-speed F-actin cosedimentation assays to analyze the F-actin binding properties of truncated LSP1 peptides and to define the F-actin binding domains. Results show that LSP1 has at least three and potentially a fourth F-actin binding domain. All F-actin binding domains are located in the basic C-terminal half and correspond to the caldesmon and villin headpiece homologous regions. LSP1 181\u2013245 and LSP1 246\u2013295, containing sequences homologous to caldesmon F-actin binding site I and II, respectively (CI, CII), binds F-actin; similarly, LSP1 306\u2013339 can bind F-actin and contains two inseparable villin headpiece-like F-actin binding domains (VI, VII). Although LSP1 1\u2013305, which does not contain VI and VII regions, retains F-actin binding activity, its binding affinity for F-actin is much weaker than that of full-length LSP1. Site-directed mutagenesis of the basic amino acids in the KRYK (VI) or KYEK (VII) sequences to acidic amino acids create mutants that bind F-actin with lower affinity than full-length wild-type LSP1. High KCl concentrations decrease full-length LSP1 binding to F-actin, suggesting the affinity between LSP1 and F-actin is mainly through electrostatic interaction.<\/jats:p>","DOI":"10.4049\/jimmunol.165.4.2052","type":"journal-article","created":{"date-parts":[[2014,4,20]],"date-time":"2014-04-20T20:29:56Z","timestamp":1398025796000},"page":"2052-2058","source":"Crossref","is-referenced-by-count":16,"title":["Human Lymphocyte-Specific Protein 1, the Protein Overexpressed in Neutrophil Actin Dysfunction with 47-kDa and 89-kDa Protein Abnormalities (NAD 47\/89), Has Multiple F-Actin Binding Domains"],"prefix":"10.1093","volume":"165","author":[{"given":"Qihong","family":"Zhang","sequence":"first","affiliation":[{"name":"Department of Cell Biology, School of Medicine, University of Alabama , Birmingham, AL 35295"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yao","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, School of Medicine, University of Alabama , Birmingham, AL 35295"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas H","family":"Howard","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, School of Medicine, University of Alabama , Birmingham, AL 35295"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2000,8,15]]},"reference":[{"key":"2026020213120603800_R1","first-page":"1093","volume-title":"N. 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