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The appendage domain of the AP-2 subunit is not required for assembly or invagination of clathrin-coated pits.

Data up to Jan 2025

Published1993
Citations75
References39

Total Citations Per Year

Abstract

References (39)

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Assembly polypeptides from coated vesicles mediate reassembly of unique clathrin coats.

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Clathrin-coated pits contain an integral membrane protein that binds the AP-2 subunit with high affinity.

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Subunit interaction and function of clathrin-coated vesicle adaptors from the Golgi and the plasma membrane.

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Coat proteins isolated from clathrin coated vesicles can assemble into coated pits.

1989 • 56 citations

Limited proteolytic digestion of coated vesicle assembly polypeptides abolishes reassembly activity

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Clathrin assembly protein AP-2 induces aggregation of membrane vesicles: a possible role for AP-2 in endosome formation.

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1991 • 40 citations

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The appendage domain of the AP-2 subunit is not required for assembly or invagination of… (1993) – The Journal of Cell Biology | Metascience Observatory Explorer