AP-2-Containing Clathrin Coats Assemble on Mature Lysosomes

Coat proteins appear to play a general role in intracellular protein trafficking by coordinating a membrane budding event with cargo selection. Here we show that the AP-2 adaptor, a clathrin-associated coat-protein complex that nucleates clathrin-coated vesicle formation at the cell surface, can als...

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Bibliographic Details
Published in:The Journal of cell biology 1996-12, Vol.135 (6), p.1801-1814
Main Authors: Traub, Linton M., Bannykh, Sergei I., Rodel, Jill E., Aridor, Meir, Balch, William E., Kornfeld, Stuart
Format: Article
Language:English
Subjects:
Animals
Antibodies
Antigens, CD - analysis
Antigens, CD - metabolism
Biochemistry
Brain - cytology
Cell Membrane Permeability
Cell membranes
Cells
Cells, Cultured - chemistry
Cells, Cultured - metabolism
Cells, Cultured - ultrastructure
Cellular biology
Clathrin - analysis
Coated Vesicles - chemistry
Coated Vesicles - ultrastructure
Cytosol
DNA-Binding Proteins - analysis
DNA-Binding Proteins - metabolism
Endosomes
Fluorescent Antibody Technique
Freeze Etching
Kidney - cytology
Liver
Liver - cytology
Lysosomal Membrane Proteins
Lysosomes
Lysosomes - chemistry
Lysosomes - metabolism
Lysosomes - ultrastructure
Membrane Glycoproteins - analysis
Membrane Glycoproteins - metabolism
Membrane Proteins - analysis
Microscopy, Electron
P branes
Proteins
Rats
Receptors
T lymphocytes
Transcription Factor AP-2
Transcription Factors - analysis
Transcription Factors - metabolism
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Description
Summary:Coat proteins appear to play a general role in intracellular protein trafficking by coordinating a membrane budding event with cargo selection. Here we show that the AP-2 adaptor, a clathrin-associated coat-protein complex that nucleates clathrin-coated vesicle formation at the cell surface, can also initiate the assembly of normal polyhedral clathrin coats on dense lysosomes under physiological conditions in vitro. Clathrin coat formation on lysosomes is temperature dependent, displays an absolute requirement for ATP, and occurs in both semi-intact cells and on purified lysosomes, suggesting that clathrin-coated vesicles might regulate retrograde membrane traffic out of the lysosomal compartment.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.135.6.1801