• Login
    View Item 
    •   Home
    • Research
    • Articles
    • View Item
    •   Home
    • Research
    • Articles
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of KAUSTCommunitiesIssue DateSubmit DateThis CollectionIssue DateSubmit Date

    My Account

    Login

    Quick Links

    Open Access PolicyORCID LibguideTheses and Dissertations LibguideSubmit an Item

    Statistics

    Display statistics

    Functional Binding of E-selectin to its Ligands is Enhanced by Structural Features Beyond its Lectin Domain

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    Aleisa%20et%20al.%20Manuscript%20JBC%20REVISED%20with%20techincal%20editor%27s%20edits.pdf
    Size:
    5.403Mb
    Format:
    PDF
    Description:
    Accepted Manuscript
    Download
    Thumbnail
    Name:
    Supplemental%20Data%20Revised-after%20Editorial%20Assistants%20edits.docx
    Size:
    14.55Mb
    Format:
    Microsoft Word 2007
    Description:
    Supplemental Data
    Download
    Type
    Article
    Authors
    Aleisa, Fajr A cc
    Sakashita, Kosuke cc
    Lee, Jae Man
    Abu Samra, Dina Bashir Kamil cc
    Al Alwan, Bader cc
    Nozue, Shuho
    Tehseen, Muhammad cc
    Hamdan, Samir cc
    Habuchi, Satoshi cc
    Kusakabe, Takahiro
    Merzaban, Jasmeen cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Chemical Engineering Program
    Laboratory of DNA Replication and Recombination
    Physical Science and Engineering (PSE) Division
    Proteomics, protein expression & cytomet
    Single-Molecule Spectroscopy and Microscopy Research Group
    KAUST Grant Number
    OCRF-2014-CRG3-2276
    Date
    2020-01-16
    Online Publication Date
    2020-01-16
    Print Publication Date
    2020-03-13
    Submitted Date
    2019-09-19
    Permanent link to this record
    http://hdl.handle.net/10754/661071
    
    Metadata
    Show full item record
    Abstract
    Selectins are key to mediating interactions involved in cellular adhesion and migration, underlying processes such as immune responses, metastasis, and transplantation. Selectins are composed of a lectin domain, an epidermal growth factor (EGF)-like domain, multiple short consensus repeats (SCRs), a transmembrane domain, and a cytoplasmic tail. It is well established that the lectin and EGF domains are required to mediate interactions with ligands; however, the contributions of the other domains in mediating these interactions remain obscure. Using various E-selectin constructs produced in a newly developed silkworm-based expression system and several assays performed under both static and physiological flow conditions, including flow cytometry, glycan array analysis, surface plasmon resonance, and cell-rolling assays, we show here that a reduction in the number of SCR domains is correlated with a decline in functional E-selectin binding to hematopoietic cell E- or L- selectin ligand (HCELL) and P-selectin glycoprotein ligand-1 (PSGL-1). Moreover, the binding was significantly improved through E-selectin dimerization and by a substitution (A28H) that mimics an extended conformation of the lectin and EGF domains. Analyses of the association and dissociation rates indicated that the SCR domains, conformational extension, and dimerization collectively contribute to the association rate of E-selectin–ligand binding, whereas just the lectin and EGF domains contribute to the dissociation rate. These findings provide the first evidence of the critical role of the association rate in functional E-selectin–ligand interactions, and they highlight that the SCR domains have an important role that goes beyond the structural extension of the lectin and EGF domains.
    Citation
    Aleisa, F. A., Sakashita, K., Lee, J. M., AbuSamra, D. B., Alwan, B., Nozue, S., … Merzaban, J. S. (2020). Functional Binding of E-selectin to its Ligands is Enhanced by Structural Features Beyond its Lectin Domain. Journal of Biological Chemistry, jbc.RA119.010910. doi:10.1074/jbc.ra119.010910
    Sponsors
    This research was supported by a King Abdullah University of Science and Technology (KAUST) Faculty Baseline Research Funding Program to J.S.M. and by a Competitive Research Grant (OCRF-2014-CRG3-2276) awarded to J.S.M. We would like to express our gratitude to Mr. Vlad-Stefan Raducanu for discussion about E-S0 sample aggregates; Ms. Maryam Mih, Ms. Samar A. Rustum and Ms. Umme Habiba for their support in the management of the lab. We would also like to thank Veronica Tremblay from the KAUST Academic Writing Service for editing the manuscript.
    Publisher
    American Society for Biochemistry & Molecular Biology (ASBMB)
    Journal
    Journal of Biological Chemistry
    DOI
    10.1074/jbc.ra119.010910
    Additional Links
    http://www.jbc.org/lookup/doi/10.1074/jbc.RA119.010910
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.ra119.010910
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program; Physical Science and Engineering (PSE) Division; Chemical Engineering Program

    entitlement

     
    DSpace software copyright © 2002-2023  DuraSpace
    Quick Guide | Contact Us | KAUST University Library
    Open Repository is a service hosted by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items. For anonymous users the allowed maximum amount is 50 search results.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.