Selective externalization of an ATP-binding protein structurally related to the clathrin-uncoating ATPase/heat shock protein in vesicles containing terminal transferrin receptors during reticulocyte maturation.
Selective externalization of an ATP-binding protein structurally related to the clathrin-uncoating ATPase/heat shock protein in vesicles containing terminal transferrin receptors during reticulocyte maturation.
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DOI：
10.1016/s0021-9258(18)66719-5
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发表时间：
1986-11
期刊：
影响因子：
--
通讯作者：
Jonathan Q. Davis;Danielle DansereauO;Rose M. Johnstone;Vann Bennett
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文献类型：
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作者：
Jonathan Q. Davis;Danielle DansereauO;Rose M. Johnstone;Vann Bennett
转铁蛋白受体从网织红细胞的囊泡中丢失，在红细胞成熟的最后阶段释放(潘，B.T.，和Johnstone，R.M.(1983)Cell 33,967-977)。含有转铁蛋白受体的囊泡的主要蛋白质组分与在十二烷基硫酸钠凝胶上迁移的受体以两种多肽的形式存在，其比例为1：1，MR=71,000和72,000。通过比较MR=72,000和71,000多肽和去包被蛋白的肽图，以及通过这些多肽与ATP-琼脂糖选择性结合，基于与针对去包被蛋白的亲和纯化抗体的交叉反应，MR=71,000/72,000双联体与去包被的ATPase/热休克蛋白没有区别。这一发现表明，与去涂层/热休克蛋白家族相关的蛋白质可能通过一种独立于溶酶体的途径处理老化的膜蛋白。
Transferrin receptors are lost from reticulocytes in vesicles that are released during the final stage of erythrocyte maturation (Pan, B. T., and Johnstone, R. M. (1983) Cell 33, 967-977). Transferrin receptor-containing vesicles have a major protein component present in a 1:1 ratio with the receptor that migrates on sodium dodecyl sulfate gels as two polypeptides of Mr = 71,000 and 72,000. The Mr = 71,000/72,000 doublet is indistinguishable from the clathrin-uncoating ATPase/heat shock protein based on cross-reaction with affinity-purified antibody against the uncoating protein, by comparison of peptide maps of the Mr = 72,000 and 71,000 polypeptides and the uncoating protein, and by selective binding of these polypeptides to ATP-agarose. This finding suggests a possible activity of proteins related to the uncoating/heat shock protein family in the disposal of aged membrane proteins by a pathway independent of lysosomes.