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PMID: 3402440 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane.

The EMBO journal ·Vol. 7 ·No. 4 ·1988-04-00 ·Pages 919-29

Ahle S, Mann A, Eichelsbacher U, Ungewickell E

Abstract

We have established by peptide mapping and immunochemical analysis of purified clathrin assembly protein preparations from 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.

MeSH Terms
Animals Brain/metabolism Cattle Cell Membrane/metabolism Clathrin/biosynthesis,genetics,isolation & purification Electrophoresis, Polyacrylamide Gel Golgi Apparatus/metabolism Macromolecular Substances Molecular Weight Peptide Fragments/analysis Protein Processing, Post-Translational
Chemicals
Clathrin Macromolecular Substances Peptide Fragments
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ahle S
Max-Planck-Institut für Biochemie, Martinsried b. München, FRG.
Mann A
Eichelsbacher U
Ungewickell E
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1988-04-00
Pages
919-29
Language
English
Region
England
NLM ID
8208664
PMCID
PMC454417
Subset
IM
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