PARTICIPATION OF ALPHA-ACTININ IN THE CAPPING OF CELL-MEMBRANE COMPONENTS

PARTICIPATION OF ALPHA-ACTININ IN THE CAPPING OF CELL-MEMBRANE COMPONENTS
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DOI:
10.1016/0092-8674(79)90202-2
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发表时间:
1979-01-01
期刊:
影响因子:
64.5
通讯作者:
SINGER, SJ
SINGER, SJ
中科院分区:
生物学1区
文献类型:
--
作者:
GEIGER, B;SINGER, SJ

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Double fluorescence staining experiments demonstrated that intracellular .alpha.-actinin accumulates under cap and patches induced in several cells by a variety of ligands. This phenomenon was demonstrated in [mouse] lymphocytes and lymphoma cells treated with anti-H[histone]2 sera; spleen lymphocytes treated with concanavalin A or anti-immunoglobulin antibodies and VSV[vesicular stomatitis virus]-infected mouse fibroblast line MC57 treated with antiserum against viral antigens. It occurred during both rapid and slow capping processes and could be obtained by either direct or indirect ligand-induced redistribution. These observations were carried out on whole cells. For other cytoskeletal proteins such as filamin, tropomyosin and myosin, a similar accumulation under caps was not readily apparent using whole cell mounts, although earlier experiments with frozen-sectioned cells showed an enrichment of myosin (and actin). The enrichment of .alpha.-actinin under the clustered surface molecules was already apparent in early stages (patches) of the capping process, with or without 10 mM NaN3 present. Prolonged incubation of the cells with different ligands resulted in endocytosis of the ligand-receptor complex. .alpha.-Actinin was not associated with the internalized complex, suggesting that it may dissociate from the patched or capped surface structures at some stage during endocytosis.