STRUCTURAL RELATIONSHIPS BETWEEN CLATHRIN ASSEMBLY PROTEINS FROM THE GOLGI AND THE PLASMA-MEMBRANE
STRUCTURAL RELATIONSHIPS BETWEEN CLATHRIN ASSEMBLY PROTEINS FROM THE GOLGI AND THE PLASMA-MEMBRANE
复制标题
DOI:
10.1002/j.1460-2075.1988.tb02897.x
复制
发表时间:
1988-04-01
期刊:
影响因子:
11.4
通讯作者:
UNGEWICKELL, E
中科院分区:
文献类型:
--
作者:
AHLE, S;MANN, A;UNGEWICKELL, E
We have established by peptide mapping and immunochemical analysis of purified clathrin assembly protein preparations for bovine brain, that the cluster of components of mol. wt 100-120 kd fall into four classes, which we term .alpha., .beta., .beta.'' and .gamma.. The .beta. and .beta.'' proteins are immunologically related and generate a series of common tryptic peptides. The same criteria reveal no such homologies between the .alpha., .beta.(.beta.'') and .gamma. polypeptides. The so-called HA-II assembly protein group contains equimolar amounts of .alpha. and .beta. class polypeptides, which are shown to interact with each other. In the HA-I group assembly protein complex .gamma. and .beta.'' class polypeptides form a stoichiometric complex. Immunofluorescence microscopy reveals that the HA-I complex is specifically associated with clathrin-coated membranes in the Golgi region of cultured cells, whereas the HA-II complex appears to be restricted to coated pits on the plasma membrane. The data lead to the tentative conclusion that the clathrin assembly proteins are involved in the recognition of the intracellular targets by uncoated vesicles.