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Location of the 100 kd‐50 kd accessory proteins in clathrin coats.
Author(s) -
Vigers G.P.,
Crowther R.A.,
Pearse B.M.
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04469.x
Subject(s) - clathrin , vesicle , biology , clathrin adaptor proteins , electron micrographs , biochemistry , membrane , electron microscope , physics , optics
We present a three‐dimensional map of the clathrin coat of coated vesicles, generated from tilt series of electron micrographs of unstained specimens embedded in vitreous ice. We have examined native placental coated vesicles and coats reassembled from their purified constituents, namely clathrin triskelions and accessory proteins of approximate mol. wts 100 kd and 50 kd. Our results show that the accessory proteins contribute a further shell of density within the double shell of the clathrin cage, extending from the terminal domains of the clathrin to the membrane of the vesicle. The thickness of the complete coat is approximately 22 nm.