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Mobility modulation by local concanavalin A binding. Selectivity toward different membrane proteins.

Y I Henis

    The Journal of Biological Chemistry
    |February 10, 1984
    PubMed
    Summary
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    Localized concanavalin A (ConA) binding selectively immobilizes lymphocyte membrane proteins. This immobilization depends on protein type, indicating specific interactions with the cell

    Area of Science:

    • Cell biology
    • Immunology
    • Biophysics

    Background:

    • Membrane proteins play crucial roles in cell signaling and function.
    • Understanding the regulation of membrane protein mobility is key to deciphering cellular processes.
    • Concanavalin A (ConA) is a lectin known to bind to cell surface glycoproteins.

    Purpose of the Study:

    • To investigate the selective immobilization of lymphocyte membrane proteins.
    • To determine the effect of localized concanavalin A (ConA) binding on membrane protein lateral mobility.
    • To explore the specificity of membrane protein interactions with the cytoskeleton.

    Main Methods:

    • Utilized fluorescence photobleaching recovery (FPR) to measure membrane protein diffusion.
    • Employed ConA coupled to fixed platelets for localized ConA receptor binding on lymphocytes.

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  • Labeled specific membrane proteins, including surface immunoglobulins, ConA receptors, and H-2Kk histocompatibility antigens, with fluorescent probes.

    • Main Results:

    • Localized ConA binding inhibited the diffusion of surface immunoglobulins and ConA receptors above a 12% surface coverage threshold.
    • The diffusion and aggregation of mouse histocompatibility antigens (H-2Kk) were unaffected by ConA platelet binding.
    • ConA-induced modulation of protein mobility propagated through the cytoskeleton, suggesting specific anchorage points.

    Conclusions:

    • Lymphocyte membrane protein immobilization by ConA is selective, not uniform.
    • The cytoskeleton plays a specific role in mediating the effects of ConA-induced cross-linking on membrane proteins.
    • These findings highlight the specificity of membrane protein-cytoskeleton interactions, allowing differential responses to external stimuli.